ID A0A2X4TS99_SALER Unreviewed; 506 AA.
AC A0A2X4TS99;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:SQI23110.1};
GN ORFNames=NCTC7307_02220 {ECO:0000313|EMBL:SQI23110.1};
OS Salmonella enterica subsp. arizonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=59203 {ECO:0000313|EMBL:SQI23110.1, ECO:0000313|Proteomes:UP000248731};
RN [1] {ECO:0000313|EMBL:SQI23110.1, ECO:0000313|Proteomes:UP000248731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC7307 {ECO:0000313|EMBL:SQI23110.1,
RC ECO:0000313|Proteomes:UP000248731};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; LS483466; SQI23110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X4TS99; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000248731; Chromosome 1.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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}; Ligase {ECO:0000313|EMBL:SQI23110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248731}.
FT DOMAIN 5..228
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 253..447
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 440
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 506 AA; 55031 MW; F978588B75E57078 CRC64;
MTQAVMLQGT ASDVGKSVLA AGLCRIFYQD GLRTAPFKSQ NMALNSGITP DGKEMGRAQI
FQAEAAGIMP DVRMNPVLLK PTSDRQAQIV LMGKVATNMD AVSYHDYKPR LREQILAVYN
SLAREYDVIV LEGAGSPAEI NLRDRDIVNM GMAEMAQCPV ILVADIDRGG VFAAIYGTLA
LLHKQERDRV KGVIINKFRG DVALLYSGIE QIESLTGVPV LGVMPWLDVD LEDEDGVALQ
NDKYRGNAPR DITIAIVQLP HISNFTDFNA LAAQPDVRIR YIRRPEALTD VDLVILPGSK
NTLSDLAWLR ESGMADAVLQ THRQGVPVMG ICGGYQMLGD TIVDEVESGL GTQPGLGLLN
TITRFAQDKT TTQVNATMSG ELPGWLAAAA GLPVRGYEIH MGETVLQEGC CTAMTLQKNG
CHVADGAVTA DGLAFGTYLH GLFDSDAFTR AVVNGLRARK GLVPSETTFC YAEHKARQFD
LLAEAMRQHI DINKIYTIMQ QHQEPV
//
