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Database: UniProt
Entry: A0A2A3XF15_9GAMM
LinkDB: A0A2A3XF15_9GAMM
Original site: A0A2A3XF15_9GAMM 
ID   A0A2A3XF15_9GAMM        Unreviewed;       457 AA.
AC   A0A2A3XF15;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Cobyrinic acid a,c-diamide synthase {ECO:0000313|EMBL:PCC22276.1};
GN   ORFNames=CIK78_09535 {ECO:0000313|EMBL:PCC22276.1};
OS   Halomonas sp. JB37.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=2024405 {ECO:0000313|EMBL:PCC22276.1, ECO:0000313|Proteomes:UP000217454};
RN   [1] {ECO:0000313|EMBL:PCC22276.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB37 {ECO:0000313|EMBL:PCC22276.1};
RX   PubMed=28644126;
RA   Bonham K.S., Wolfe B.E., Dutton R.J.;
RT   "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL   Elife 6:e22144-e22144(2017).
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:PCC22276.1}.
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DR   EMBL; NRGW01000001; PCC22276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3XF15; -.
DR   OrthoDB; 9764035at2; -.
DR   Proteomes; UP000217454; 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; cd05388; CobB_N; 1.
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}.
FT   DOMAIN          14..191
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          249..430
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   REGION          385..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  48547 MW;  9C45637CAD731F18 CRC64;
     MTTSLPSASC PALFIAAPSS GQGKTTVTAG LARLLRNQGK VVRVFKTGPD YLDPQILAQA
     SGQPVDQLDL WMAGEAYCRQ RFYQAAVSAD IILVEGAMGL FDGEPSSADL AALFELPLVI
     VMDVKGMAQT AAALMSGLAG FRDDLLIAGM IANACGTQRH RELIESALPP SIPLLAALPR
     DPALTLPERH LGLVQADEIR DDLEARFEAA ASALDAAGLA TALMKIAPVT FTAAQGHVPS
     VPSSLAGQTI GVAKDAAFSF IYQANLDLLE QMGAKLCFFS PLSERRLPLC DALWLPGGYP
     ELHASTLAEN ASMREDIQRF YSAGKPILAE CGGMLYCLDT LTDYDENTHT MLGLLPGQGA
     MRGRRGCQGM QTADLAEGAL RGHAHHRSMA EGTPEPIAHG RRQRHPAPGE PIYRQRQLTA
     SYLHFFFPNN PAAVASLFSG SAASAQPSAT EEFNACS
//
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