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UniProtKB/Swiss-Prot entry P16618


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HEM1_BACSU
Primary accession number P16618
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 79)
Name and origin of the protein
Protein name Glutamyl-tRNA reductase
Synonyms GluTR
EC 1.2.1.70
Gene name
Name: hemA
OrderedLocusNames: BSU28170
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2110138 [NCBI, ExPASy, EBI, Israel, Japan]
Petricek M., Rutberg L., Schroeder I., Hederstedt L.;
"Cloning and characterization of the hemA region of the Bacillus subtilis chromosome.";
J. Bacteriol. 172:2250-2258(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969504 [NCBI, ExPASy, EBI, Israel, Japan]
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.;
"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.";
Microbiology 142:3067-3078(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M57676; AAA22510.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75208; CAA99543.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99118; CAB14777.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35252; A35252.
RefSeq NP_390695.1; -.
3D structure databases
HSSP Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]
ModBase P16618.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2813-MON; -.
Organism-specific databases
SubtiList BG10340; hemA. [Micado]
Ontologies
GO
GO:0008883; Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0006779; Biological process: porphyrin biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00087; -; 1.
PBIL [Tree]
InterPro IPR000343; 4pyrrol_synth_GluRdtase.
IPR015896; 4pyrrol_synth_GluRdtase_C.
IPR015895; 4pyrrol_synth_GluRdtase_N.
IPR016040; NAD(P)-bd.
IPR003462; ODC_Mu_crystall.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR13812; ODC_Mu_crystall; 1.
Pfam PF00745; GlutR_dimer; 1.
PF05201; GlutR_N; 1.
PF01488; Shikimate_DH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000445; 4pyrrol_synth_GluRdtase; 1.
TIGRFAMs TIGR01035; hemA; 1.
PROSITE PS00747; GLUTR; 1.
BLOCKS P16618.
Genome annotation databases
GeneID 937443; -.
GenomeReviews AL009126_GR; BSU28170.
KEGG bsu:BSU28170; -.
NMPDR fig|224308.1.peg.2820; -.
Phylogenomic databases
HOGENOM P16618; -.
Genome annotation databases
CMR P16618; BSU28170.
Other
ProtoNet P16618.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   455  455     Glutamyl-tRNA reductase. PRO_0000113996
NP_BIND   189   194  6     NADP (By similarity). 
REGION   49    52  4     Substrate binding (By similarity). 
REGION   114   116  3     Substrate binding (By similarity). 
ACT_SITE   50    50        Nucleophile (By similarity). 
BINDING   109   109        Substrate (By similarity). 
BINDING   120   120        Substrate (By similarity). 
SITE   99    99  1     Important for activity (By similarity). 
MUTAGEN   105   105        C->Y: Loss of activity. 
Sequence information
Length: 455 AA [This is the length of the unprocessed precursor] Molecular weight: 50844 Da [This is the MW of the unprocessed precursor] CRC64: B7AD817A5244A629 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHILVVGVDY KSAPIEIREK VSFQPNELAE AMVQLKEEKS ILENIIVSTC NRTEIYAVVD 

        70         80         90        100        110        120 
QLHTGRYYIK KFLADWFQLS KEELSPFLTF YESDAAVEHL FRVACGLDSM VIGETQILGQ 

       130        140        150        160        170        180 
VRDSFKTAQQ EKTIGTIFNE LFKQAVTVGK RTHAETDIGS NAVSVSYAAV ELAKKIFGNL 

       190        200        210        220        230        240 
SSKHILILGA GKMGELAAEN LHGQGIGKVT VINRTYLKAK ELADRFSGEA RSLNQLESAL 

       250        260        270        280        290        300 
AEADILISST GASEFVVSKE MMENANKLRK GRPLFMVDIA VPRDLDPALN DLEGVFLYDI 

       310        320        330        340        350        360 
DDLEGIVEAN MKERRETAEK VELLIEETIV EFKQWMNTLG VVPVISALRE KALAIQSETM 

       370        380        390        400        410        420 
DSIERKLPHL STREKKLLNK HTKSIINQML RDPILKVKEL AADADSEEKL ALFMQIFDIE 

       430        440        450 
EAAGRQMMKT VESSQKVHSF KKAESKAGFS PLVSE 

P16618 in FASTA format

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