ID A0A2S1JS01_9GAMM Unreviewed; 502 AA.
AC A0A2S1JS01;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=BTJ40_10310 {ECO:0000313|EMBL:AWF81179.1};
OS Microbulbifer sp. A4B17.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=359370 {ECO:0000313|EMBL:AWF81179.1, ECO:0000313|Proteomes:UP000244764};
RN [1] {ECO:0000313|EMBL:AWF81179.1, ECO:0000313|Proteomes:UP000244764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4B17 {ECO:0000313|EMBL:AWF81179.1,
RC ECO:0000313|Proteomes:UP000244764};
RX PubMed=16885309; DOI=10.1128/AEM.00494-06;
RA Peng X., Adachi K., Chen C., Kasai H., Kanoh K., Shizuri Y., Misawa N.;
RT "Discovery of a marine bacterium producing 4-hydroxybenzoate and its alkyl
RT esters, parabens.";
RL Appl. Environ. Microbiol. 72:5556-5561(2006).
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000256|ARBA:ARBA00025166, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
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DR EMBL; CP029064; AWF81179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1JS01; -.
DR KEGG; mii:BTJ40_10310; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000244764; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05389; CobQ_N; 1.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00313; cobQ; 1.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00028};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00028}.
FT DOMAIN 4..230
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 249..442
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 502 AA; 54295 MW; CB697D5C1E9BF84C CRC64;
MSVLMVQGTT SDAGKSTLVA GLARYFSLRG VSVAPFKPQN MALNSAVTVD GGEIGRAQAL
QALACGVDPH SDMNPVLLKP ASDTGAQVII QGKVLGNMQA LDYHHYKATA QNAVLDSFAR
LDDQYELVLV EGAGSPAEIN LRENDIANMG FAEAVDCPVI LIADIDRGGV FAHLVGTLEL
LSSSERERVV GFVINRFRGD LQLLQPGLDW LEEYTGKPVL GVLPYLHDLY LDAEDAISTQ
QSGADARLKV VVPLLPRISN HTDFDALRLH PDIDLQFVSV REPVPQCDWI ILPGSKNVRA
DLAYLKENDW PAQLDRHLRY GGKLVGICGG LQMLGSEVQD PDGVEDTPGN EPGLGYLDFT
TRLQPVKALK NITGFLALEN EVKEAAPVQG YEIHCGITEG VALQTPAVYI CDKDGNSRPD
GAISADGQVF ATYVHGLFDS PEALSALFAW GGLKDSTPLD VGEQRQQQLD RLAETIAENI
QGNWLEQFEG TRETAALQED SQ
//
