ID A0A2U9TCM0_9GAMM Unreviewed; 430 AA.
AC A0A2U9TCM0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cobyrinic acid a, c-diamide synthase {ECO:0000313|EMBL:AWV08228.1};
GN ORFNames=C9I47_2551 {ECO:0000313|EMBL:AWV08228.1};
OS Lysobacter maris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1605891 {ECO:0000313|EMBL:AWV08228.1, ECO:0000313|Proteomes:UP000249447};
RN [1] {ECO:0000313|EMBL:AWV08228.1, ECO:0000313|Proteomes:UP000249447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ9B {ECO:0000313|EMBL:AWV08228.1,
RC ECO:0000313|Proteomes:UP000249447};
RA Zhang X.-Q.;
RT "The complete genome of Lysobacter maris HZ9B, a marine bacterium
RT antagonistic against terrestrial plant pathogens.";
RL Submitted (MAY-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}.
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DR EMBL; CP029843; AWV08228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9TCM0; -.
DR KEGG; lmb:C9I47_2551; -.
DR OrthoDB; 9764035at2; -.
DR Proteomes; UP000249447; Chromosome.
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 Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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 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:UP000249447}.
FT DOMAIN 11..187
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 239..420
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 430 AA; 45537 MW; DA544B6FBAD9A27A CRC64;
MEAARCPALL VSAPASGQGK TSVTAALARW HRRNGRRVRV FKTGPDFLDP MILERASGAP
VQQLDLWMCG EADVRARLHA AAREADLILV EGVMGLFDGA PSSADLALAL GLPVLAVIDG
AAMAQTFGAL ATGLAKYREG LRVHGIAANR IGSAHHARLL RDSLPAEIAW MGALPRSPEL
ALPERHLGLV AAAELADLDA RLDALADAWG EHATTALPPP IGFADVEPLP VPRRLEGWRI
AVARDAAFCF LYPANLALLR EAGAELSFFS PVAGDALPEC DAAWLPGGYP ELHLDALAAN
TGLHAALRAH RDAGKPLLAE CGGLLFALRS LVDRDGRGAS MAGLIAGEAR MQPRFAALGM
QEVELPEGTL RGHSFHYARA DIEATPLTLA RNPNGGPTAE AVYRDRGMTA SFVHLYFASN
PEAAVRLLRP
//
