ID A0A269PJZ2_9GAMM Unreviewed; 512 AA.
AC A0A269PJZ2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=CJF42_20390 {ECO:0000313|EMBL:PAJ72583.1};
OS Pseudoalteromonas sp. NBT06-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=2025950 {ECO:0000313|EMBL:PAJ72583.1, ECO:0000313|Proteomes:UP000215836};
RN [1] {ECO:0000313|EMBL:PAJ72583.1, ECO:0000313|Proteomes:UP000215836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBT06-2 {ECO:0000313|EMBL:PAJ72583.1,
RC ECO:0000313|Proteomes:UP000215836};
RA Wei Y.;
RT "Pseudoalteromonas hadalis sp. nov., a facultative psychrophile isolated
RT from New Britain Trench.";
RL Submitted (AUG-2017) 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:PAJ72583.1}.
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DR EMBL; NQMR01000135; PAJ72583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A269PJZ2; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000215836; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000215836}.
FT DOMAIN 1..225
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 245..455
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 449
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 512 AA; 56023 MW; 6CB98462732D9F83 CRC64;
MVQGTTSDAG KTTLVCGLGR VFKRKGIKVA PFKPQNMALN SAVTIDGGEI GRAQALQAQA
CNLEPVCDFN PVLLKPSSDI GCQVIINGQI AAQLDAQNYH DYKPTAMKAV LKAHKRLAEK
FESILVEGAG SPAEINLRDR DIANMGFAEE VDCPVILIAD IDKGGVFAHL TGTLACLSES
EQNRVIGFVI NRFRGDAALL TSGLDWLEEQ TGKPVLGVLP YLQGLHLDSE DSVALEQVID
KPKLNVVIPV YPRTSNHNDF DSLRAHPDVN VQLVGPQLMR AQATNSELQS NKPKADLLIL
PGSKNTQADL TWFKEQGWEE YIKRHLRYDG KVLAICGGLQ MLGIEIKDPN GIESPQCKTT
QGLGLLPLIT TLQANKALSL KKGMLQLPGQ NKVAIQGYEI HTGNTFIVDE PLNNLADIQQ
VVFDNDELNA CFGSGVISED NQIFASYWHG LMDTPEALTA ILNWATDSVI GSGFKHVDYQ
ALREHSINHL ADNIEQEFDW NKLTAALKKF NR
//
