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Database: UniProt
Entry: G9Z9R0_9ENTR
LinkDB: G9Z9R0_9ENTR
Original site: G9Z9R0_9ENTR 
ID   G9Z9R0_9ENTR            Unreviewed;       497 AA.
AC   G9Z9R0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
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=HMPREF0880_04267 {ECO:0000313|EMBL:EHM45312.1};
OS   Yokenella regensburgei ATCC 43003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Yokenella.
OX   NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM45312.1, ECO:0000313|Proteomes:UP000003044};
RN   [1] {ECO:0000313|EMBL:EHM45312.1, ECO:0000313|Proteomes:UP000003044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM45312.1,
RC   ECO:0000313|Proteomes:UP000003044};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHM45312.1}.
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DR   EMBL; AGCL01000044; EHM45312.1; -; Genomic_DNA.
DR   RefSeq; WP_006820716.1; NZ_JH417874.1.
DR   AlphaFoldDB; G9Z9R0; -.
DR   STRING; 1002368.HMPREF0880_04267; -.
DR   PATRIC; fig|1002368.3.peg.3898; -.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000003044; 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; 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          2..222
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          248..437
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   497 AA;  54045 MW;  5E0137B5BD4AA42E CRC64;
     MLQGTASDVG KSVLVAGLCR IFHQDGLKSA PFKSQNMALN SGITDDGKEM GRAQIFQAEA
     AGIRPDVRMN PILLKPTTDR QAQVVLMGEV AQSMDAVSYH HYKPQLRETI LGAWRSLAEA
     FDVLVLEGAG SPAEINLRDR DIVNMGMAEM AECPVILVAD IDKGGVFASI YGTLALLQES
     ERWRVKGVII NKFRGDVSLL QSGLEQIESL TGVPVLGVMP WLNVDLEEED GVALQYRRAR
     LSPEASVNIA VVEFPHIANF TDFNPLSAQP GVNVHYVRHP EALADCDLII LPGSKNTLGD
     LDWLRQTAMA QAVLEAHRCG VPVIGVCGGY QMMGDVIFDE IESGMGRQSG LGLLNATTRF
     EAVKTTVQTT VRLSDNLPGW LAPLSGLSLN GYEIHMGQTT LQAGCQKAMQ YDTALGAVDD
     SGLAFGTYLH GLFDNDAFTG GVVNSLRARK GLPQQTVVQS YADYKAQQFD VLAAGMRENI
     DIQRIYQIMR EHQEPTV
//
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