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Database: UniProt
Entry: A0A1G5AXP6_9FIRM
LinkDB: A0A1G5AXP6_9FIRM
Original site: A0A1G5AXP6_9FIRM 
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
//
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