ID A0A2T3N0W8_9GAMM Unreviewed; 444 AA.
AC A0A2T3N0W8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cobyrinate a,c-diamide synthase {ECO:0000313|EMBL:PSW05977.1};
GN ORFNames=C9I89_05500 {ECO:0000313|EMBL:PSW05977.1};
OS Photobacterium lipolyticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=266810 {ECO:0000313|EMBL:PSW05977.1, ECO:0000313|Proteomes:UP000240904};
RN [1] {ECO:0000313|EMBL:PSW05977.1, ECO:0000313|Proteomes:UP000240904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16190 {ECO:0000313|EMBL:PSW05977.1,
RC ECO:0000313|Proteomes:UP000240904};
RA Butler K.;
RT "Whole genome sequencing of Histamine producing bacteria.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205}.
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:PSW05977.1}.
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DR EMBL; PYMC01000003; PSW05977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3N0W8; -.
DR OrthoDB; 9764035at2; -.
DR Proteomes; UP000240904; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03130; GATase1_CobB; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR004484; CbiA/CobB_synth.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00379; cobB; 1.
DR PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00606};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000240904}.
FT DOMAIN 11..189
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 241..429
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 444 AA; 48234 MW; E187767E4101C849 CRC64;
MSNSTVQCPA LVVTAPSSGS GKTTVVAALA RHFHLQGKKV RVFKTGPDFI DPRFLEFASQ
QPVYQLDFWM CGEKHCKALI AEAAKEADLI LIEGVMGMFD GHCSSADIAA RLGIPVLAVI
DAGAMAQTFG ALAYGLANYR DDIEMFGVVA NRVGSVHHAQ MLQESLPENL AFCGWLPKES
GITLPERHLG LVQADELEDL DQRLDRAAEL IGEFGKVTLP PPMAFDDVSA DKVTSHLAGK
TIAIARDRAF SFIYRANIDL LQAMGADVQF FSPISGDCLP DCDALYLPGG YPELSTGALA
ENQTLIAQIK QHVEQGKPCL AECGGMLYLN RSLTMLDGTT AILSDVLDAD SAMQPKLAAL
GMVEAAFSYN NDTCNNSHTL RGHTFHYSTT QSNEQVLTQP VSQRGRKTDP VWFKNNLIAS
YIHWYFPSNP KLVADIFSGK VSEQ
//