ID F6EIZ9_AMYSD Unreviewed; 467 AA.
AC F6EIZ9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 29-MAY-2013, entry version 12.
DE RecName: Full=Cobyrinic acid A,C-diamide synthase;
GN Name=cobB; OrderedLocusNames=AS9A_1611;
OS Amycolicicoccus subflavus (strain DSM 45089 / DQS3-9A1).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Amycolicicoccus.
OX NCBI_TaxID=443218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1;
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- FUNCTION: Responsible for the amidation of carboxylic groups at
CC position A and C of either cobyrinic acid or hydrogenobrynic acid.
CC NH(2) groups are provided by glutamine, and one molecule of ATP is
CC hydrogenolyzed for each amidation (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobB subfamily.
CC -!- SIMILARITY: Contains 1 GATase cobBQ-type domain.
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DR EMBL; CP002786; AEF40060.1; -; Genomic_DNA.
DR RefSeq; YP_004492860.1; NC_015564.1.
DR EnsemblBacteria; AEF40060; AEF40060; AS9A_1611.
DR GeneID; 10633784; -.
DR KEGG; asd:AS9A_1611; -.
DR KO; K02224; -.
DR BioCyc; ASUB443218:GH9R-1639-MONOMER; -.
DR UniPathway; UPA00148; -.
DR GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:HAMAP.
DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:HAMAP.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:HAMAP.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:HAMAP.
DR HAMAP; MF_00027; CobB; 1; -.
DR InterPro; IPR004484; CbiA_synth.
DR InterPro; IPR017929; CobB/CobQ_GATase.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00379; cobB; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Complete proteome; Glutamine amidotransferase.
FT DOMAIN 257 443 GATase cobBQ-type (By similarity).
FT ACT_SITE 339 339 Nucleophile (By similarity).
FT ACT_SITE 435 435 By similarity.
SQ SEQUENCE 467 AA; 48274 MW; A3DEEAC6CED860EE CRC64;
MTVPAVVLAA PSSGSGKTTL ATGIMAALRA SGLRVAPFKV GPDYIDPGYH SLATGRPGRN
LDPVLTSPEL VGPLFQHGSA GCDIAIVEGV MGLFDGRIGS AELAEGSTAQ VAALLGAPVV
LVVDVRGHSQ SLAALLHGFA TFDPRVRIAG VILNQVGSDR HEHVLREACD RAGMPVLGVV
PRDGNVSLPS RHLGLVTAAE HGGAADAAIR AMGELARSCI DLPGLRQIAR SAVLAEAWSP
GGALGESSGA GYQRRPVIAV ASGPAFTFRY AEHDELLRAA GADIAVFDPL SDGLPEGTTG
IVLPGGFPEL YAAALAENVA LLSQVRDAAA AEVPIVAECA GLLYLSRKVD LYPMAGVIAA
DAVFGKRLVL GYRDAAALSD SVAFRAGERV TGHEFHRTHL LENERTDAAW GWRDHAGALV
REGFVGNSVH ASYLHTHPAG HPSSVARFVA AARAKQPVVE SRPAIAP
//
