ID A0A0C4YQ09_9BURK Unreviewed; 452 AA.
AC A0A0C4YQ09;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cobyrinic acid A,C-diamide synthase {ECO:0000313|EMBL:AJG24580.1};
GN ORFNames=RR42_s2999 {ECO:0000313|EMBL:AJG24580.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG24580.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG24580.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG24580.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010537; AJG24580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4YQ09; -.
DR STRING; 68895.RR42_s2999; -.
DR KEGG; cbw:RR42_s2999; -.
DR Proteomes; UP000031843; Chromosome secondary.
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; cd03130; GATase1_CobB; 1.
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:UP000031843}.
FT DOMAIN 29..184
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 259..440
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 452 AA; 46656 MW; ED2F188793181102 CRC64;
MPNLAATVAS AVPGTRTDAA RSLRVPAMLV AAPASGQGKT TVTAALAWLH RRAGRTVRVF
KSGPDYLDPS ILAAASGAPV HSLDLWMTGA EDAAARLAKA AAEADLILVE GVMGLHDGTP
SSADLARHFG LPVLSVIQAG AMAQTFGALA FGLAGYGQPL ASMQVLANGV ASPRHADMLQ
ESLPAHIGWA GALARDNAAS LPERHLGLLA ADELPDLNTR LDRLADALAG QPIGALPAAV
EIAAAPPLPV LPPLLAGKTI AIARDAAFRF LYPANLDTLQ ALGARLAFFS PLDDATLPDC
DALWLPGGYP ELHAARLSAN TGMLAALRQA HADSLPILAE CGGMMALFET LVDKAGDSHA
VAGLLPGTVT MQRRLAALGH QQLALPEGTL RGHTFHYSSA QTPLAPYCHA TVPRDGSRGE
AVFRQGALTA SYTHLYFPSN PLAIAALLSG VR
//
