ID A0A1G5AXP6_9FIRM Unreviewed; 442 AA.
AC A0A1G5AXP6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Cobyrinic acid a,c-diamide synthase {ECO:0000313|EMBL:SCX82657.1};
GN ORFNames=SAMN05660668_00446 {ECO:0000313|EMBL:SCX82657.1};
OS Pseudobutyrivibrio sp. AR14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520804 {ECO:0000313|EMBL:SCX82657.1, ECO:0000313|Proteomes:UP000198746};
RN [1] {ECO:0000313|EMBL:SCX82657.1, ECO:0000313|Proteomes:UP000198746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR14 {ECO:0000313|EMBL:SCX82657.1,
RC ECO:0000313|Proteomes:UP000198746};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; FMUY01000002; SCX82657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5AXP6; -.
DR Proteomes; UP000198746; Unassembled WGS sequence.
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 Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004484; CbiA_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 4: Predicted;
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}.
FT DOMAIN 1..184
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 245..390
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 442 AA; 48839 MW; A4CA8B1ECF1DCE78 CRC64;
MLAANKSGSG KTTITCGLLG ALKERGLNPC SFKCGPDYID PMFHRNVLGI PSGNLDTFFT
EDDVTRELFE NEFSGDIAVI EGVMGLFDGI GGVELTGSSY DLARVLKTPI ILVIDAKGAG
RSVLAEIRGF LDYDREHLIK GVILNRTSKA FGVKLADLIE EELHIKCFGT VAEEKNVELS
SRHLGLYLPQ EIDDINKKLE KQTNLVLDGV DIDGIIELSK TVPEIKAASK IFVQPSKASD
NKLRLGVARD EAFCFYYREN LAMLQARGVE LVEFSPLRDH HLPENISGIL LGGGYPENYL
SALQGNTQIK AEIKKAMDRG IPMLAECGGF MYLLDNIKNE QDKTYNMIGA INGSAYWTGK
LVRFGYVTIE AEGFEIKGHE FHYYDTDNNG SSFTAKKPTG NRSWQCIHKV GPSYIGFPHL
YYPSAPVFVD KFVEAMKNYG GN
//