ID A0A4E0QTK8_9GAMM Unreviewed; 429 AA.
AC A0A4E0QTK8;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Cobalamin biosynthesis protein CobB {ECO:0000313|EMBL:TGO03040.1};
GN ORFNames=PN36_13680 {ECO:0000313|EMBL:TGO03040.1};
OS Candidatus Thiomargarita nelsonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiomargarita.
OX NCBI_TaxID=1003181 {ECO:0000313|EMBL:TGO03040.1, ECO:0000313|Proteomes:UP000030428};
RN [1] {ECO:0000313|EMBL:TGO03040.1, ECO:0000313|Proteomes:UP000030428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hydrate Ridge {ECO:0000313|EMBL:TGO03040.1};
RX PubMed=27199933; DOI=10.3389/fmicb.2016.00603;
RA Flood B.E., Fliss P., Jones D.S., Dick G.J., Jain S., Kaster A.K.,
RA Winkel M., Mussmann M., Bailey J.;
RT "Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita
RT nelsonii Reveals Genomic Plasticity.";
RL Front. Microbiol. 7:603-603(2016).
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:TGO03040.1}.
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DR EMBL; JSZA02000046; TGO03040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4E0QTK8; -.
DR Proteomes; UP000030428; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000030428}.
FT DOMAIN 6..169
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 241..416
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 429 AA; 47387 MW; 06663C68977BDBCE CRC64;
MNYALIGGTQ SGCGKTSVTL ALLQFLNKRQ KSVRCFKTGP DFLDPMWHKA ITHKTSYNLD
TNMMAIEQIQ QILSKHQDVE FGIIEGVMGL FDGKSGVGGK GSAAHLAKVL DVPVWLVVNA
KGMSGSIVPL VKGFVREAED IGFRISGIIA NRLGSENHAR IIRELLLEHQ LPPLIAWMEK
NAPLLSERHL GLQMPEEHDV PDFSKAFHVE LDLLKSTSDS LALTSEPQIN KSKLNYLQGK
TIAVARDSAC CFIYPSNLDW LQAQAAKIIF FSPIAGDAVP DNTDAIWLPG GYPELHLQAL
SQSATWASLA KHIEQGTPTL AECGGMMLLA ESIIDHQGTS WNMAGILPIA CRMQDRLAAL
GYRQDENSGI KGHEYHHSKR EDHQILPKAY SLKRGDEGLL FNNCRASYIH WYFESAPDVA
AQLFLRKPP
//
