ID A0A1G9PDM8_9BURK Unreviewed; 484 AA.
AC A0A1G9PDM8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cobyrinic acid a,c-diamide synthase {ECO:0000313|EMBL:SDL96653.1};
GN ORFNames=SAMN05428957_101336 {ECO:0000313|EMBL:SDL96653.1};
OS Oryzisolibacter propanilivorax.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Oryzisolibacter.
OX NCBI_TaxID=1527607 {ECO:0000313|EMBL:SDL96653.1, ECO:0000313|Proteomes:UP000198552};
RN [1] {ECO:0000313|Proteomes:UP000198552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPL6 {ECO:0000313|Proteomes:UP000198552};
RA Varghese N., Submissions S.;
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};
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; FNHP01000001; SDL96653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9PDM8; -.
DR STRING; 1527607.SAMN05428957_101336; -.
DR OrthoDB; 9764035at2; -.
DR Proteomes; UP000198552; 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 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:UP000198552}.
FT DOMAIN 11..168
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 258..470
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 388..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 50776 MW; B4B333C1B6AB9FA2 CRC64;
MSAPSARCPA LVVAAPASGQ GKTTVVAALA RLHARAGRRV RVFKCGADYL DPHWHELASG
APVHPLDLWM TGEADCRQRL HAAAAEADLI LVEGVMGLFD GDASVAALAR RLGIPVLAVI
DAHAMGGTFG ALALGLRSYW PDLPWAGVLA NRVAGERHAR MLQDGLRSAS DWLGALPPVS
IAGEGRGKPG GLLPERQLGL VAARELPDAL VRLDAAANAL AATPLGMLSP RDWQRWAVDF
AAPPDAPAAP APLLAGRRVA VARDAAFCLV YEANLQTLRQ LGAQVEIFAP LQGEPLPACD
ALWLPGGFPE LHASALASLT HLREQLRRHI AAGRPVWAEG GGMLALLQSV TLADGCCLPL
WDLLPGHATL RQRLQGLGPR SWQPVADGAQ SLAKKQAPTA ARRLPDATPA APVADGALRG
HTFHYSSVDA PDLAITGHAV RPAPEEAQAG AEPVYRHGSV HASYFHAWFP SAPRAVARLL
GATP
//
