ID K0HUZ8_9BURK Unreviewed; 464 AA.
AC K0HUZ8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=CobB/CobQ domain-containing protein glutamine amidotransferase {ECO:0000313|EMBL:AFU46793.1};
GN ORFNames=C380_15495 {ECO:0000313|EMBL:AFU46793.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU46793.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU46793.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU46793.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003872; AFU46793.1; -; Genomic_DNA.
DR AlphaFoldDB; K0HUZ8; -.
DR STRING; 358220.C380_15495; -.
DR KEGG; ack:C380_15495; -.
DR PATRIC; fig|358220.3.peg.3156; -.
DR eggNOG; COG1797; Bacteria.
DR HOGENOM; CLU_022752_0_2_4; -.
DR Proteomes; UP000006306; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 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};
KW Transferase {ECO:0000313|EMBL:AFU46793.1}.
FT DOMAIN 19..176
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 266..449
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 464 AA; 48650 MW; CF8169822B795E31 CRC64;
MGAAVTLATA TAARCPALLI AAPASGQGKT TVTAALARLH ARQGRRVRVF KCGPDFLDPH
WHQLASGAPV HQLDLWMNGE ADCAHRLHDA ARESDLILIE GVMGLFDGNP SAADLARHFA
VPVLAVVDAS AMAGTFGALA YGLRHYRPGL PWAGVLANRV GSARHADMLR DGLHDVDDWM
GALMRVQPGA ASAAGNAGAA LLPERHLGLV AAHELHDSQQ RLDAAADALA ATPLGQMTLE
DMQRWAVDFP VPASKIAAPA LLAGRTVAVG RDAAFCFTYA ANVQCLEQMG ARVAFFSPLQ
DTALPDCDAV WLPGGYPELH TAQIAANTGM LASLRAHVAA GKPLWAECGG MMALFDSITL
ADGSAAPLWG LLPGRVTMQK RLAALGPQQL TVAGHTLRGH TFHYSTSDSS APVVARTARP
HEAVAPDEGE ALYQQGSIHA SYFHAWFPSS PEAVAHLLGG QSKA
//
