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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A.,
Lucas S.,
Lapidus A.,
Barry K.,
Detter J.C.,
Glavina del Rio T.,
Hammon N.,
Israni S.,
Dalin E.,
Tice H.,
Pitluck S.,
Singan V.,
Schmutz J.,
Larimer F.,
Land M.,
Hauser L.,
Kyrpides N.,
Anderson I.J.,
Miller C.,
Richardson P.;
"Complete sequence of Mycobacterium vanbaalenii PYR-1.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively (By similarity).
- CATALYTIC ACTIVITY: 3-(2,3-dihydroxyphenyl)propanoate + O2 = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate.
- CATALYTIC ACTIVITY: 2,3-dihydroxicinnamic acid + O2 = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate.
- COFACTOR: Fe(2+) ion (By similarity).
- PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid degradation.
- SUBUNIT: Homotetramer (By similarity).
- SIMILARITY: Belongs to the ligB/mhpB extradiol dioxygenase family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 316 AA [This is the length of the unprocessed precursor] |
Molecular weight: 33277 Da [This is the MW of the unprocessed precursor] |
CRC64: E05DD6995015778B [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAKSQMALCC MSHSPLLNLP GPAQELLDDI EGAIAAAREF VAAFDPDLVV TFSPDHYNGF
70 80 90 100 110 120
FYRAMPPFCV GTAAAGVGDY GTYQGPLDVP ADLAIDCARA VLDSDVDVAV SAAMDVDHGT
130 140 150 160 170 180
VQPLQKLFGD ATAKPVIPVF VNSVATPLGP MRRVRALGAA VGTHLAGLGK RVLVIGSGGL
190 200 210 220 230 240
SHDPPVPTLA TAPPAALDRI VRGVPMTTEQ RQARQAAVIE AAREFASGQG ALAPLNPDWD
250 260 270 280 290 300
RAFLDLLDNG RLAEVDSWDN RWIAEQAGNS AHEVRTWVAA FAALAAQGKY ETGNRYYRAA
310
PELIAGFAIR TAVCTS
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A1TCX1 in FASTA format |
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