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Database: UniProt
Entry: A0A0P1F709_THAGE
LinkDB: A0A0P1F709_THAGE
Original site: A0A0P1F709_THAGE 
ID   A0A0P1F709_THAGE        Unreviewed;       487 AA.
AC   A0A0P1F709;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ECO:0000313|EMBL:CUH63736.1};
GN   ORFNames=TG4357_00858 {ECO:0000313|EMBL:CUH63736.1};
OS   Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH63736.1, ECO:0000313|Proteomes:UP000051587};
RN   [1] {ECO:0000313|EMBL:CUH63736.1, ECO:0000313|Proteomes:UP000051587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH63736.1,
RC   ECO:0000313|Proteomes:UP000051587};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; CYSA01000010; CUH63736.1; -; Genomic_DNA.
DR   RefSeq; WP_058261648.1; NZ_FOFW01000012.1.
DR   AlphaFoldDB; A0A0P1F709; -.
DR   STRING; 53501.SAMN04488043_11294; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000051587; Unassembled WGS sequence.
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; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051587}.
FT   DOMAIN          5..237
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          250..434
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   487 AA;  51732 MW;  6A5EC3D75672B908 CRC64;
     MAKAIMIQGA GSNVGKSMVV AGIARALANR GLSVRPFKPQ NMSNNAAVTE DGGEIGRAQA
     LQALAARVAP HTDMNPVLLK PETDTGAQVI VQGKLFATLR ARDYSKSKPD LMRPTLESFQ
     RLCDGADIVV VEGAGSPAEV NLRRGDIANM GFAEAAGVPV ILLGDIDRGG VIAQIVGTQT
     ILPEADAARI KGFAINKFRG DVRLFDDGMT VITQRTGWPS LGVLPWFADA WRLPAEDVMD
     IASSKGDGFK IAVPRLGRIA NFDDLDPLAA EPGVSVDIIE PGRALPGDAD MVLIPGSKST
     IADLADFRAQ GWDIDLKAHI RRGGHVLGIC GGYQMLGREI SDPDGIEGGP ETVPGLGLLD
     VVTVMTPQKR LALSRATYLP SGAPVEGYEI HLGETTGPDC ARAWLDLSGR AEGASSRNGQ
     VRGCYLHGLF GSDAFRAAYL SQLGAQVQVA YSDELDAVLD RLAVHIETHF DLDLLLRLAQ
     RPRYCNS
//
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