ID A0A168Y684_9PROT Unreviewed; 408 AA.
AC A0A168Y684;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:ANC91821.1};
GN ORFNames=A6A40_07805 {ECO:0000313|EMBL:ANC91821.1};
OS Azospirillum humicireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC91821.1, ECO:0000313|Proteomes:UP000077405};
RN [1] {ECO:0000313|EMBL:ANC91821.1, ECO:0000313|Proteomes:UP000077405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC91821.1,
RC ECO:0000313|Proteomes:UP000077405};
RX PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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; CP015285; ANC91821.1; -; Genomic_DNA.
DR RefSeq; WP_063634905.1; NZ_CP015285.1.
DR AlphaFoldDB; A0A168Y684; -.
DR STRING; 1226968.A6A40_07805; -.
DR KEGG; ahu:A6A40_07805; -.
DR OrthoDB; 9808822at2; -.
DR Proteomes; UP000077405; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03112; CobW-like; 1.
DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR011629; CobW-like_C.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13748:SF62; COBW DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; CobW_C; 1.
DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 309..403
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 241..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 44830 MW; 396A635F8CD7CB68 CRC64;
MQILSGETPL SAPAASPARL PVSVLTGFLG SGKTTLLQAL LRNPGMARTA IVINEFGEVG
LDHLLVAKAS ENMVLMDSGC LCCTIRGDLV DTLRDLFLKR VKGEIPDFDR VVVETTGLAD
PAPIIHTLMS DPLLAARFRL DGVIATVDAA HGSLQLDRQP ESVKQAAVAD RIVLTKTDVA
TPAATAALMQ RLAAINPAAP VLPAAHGEID PKRLFDAGLY NPETKSPDVA RWLREEAYRD
EQAKAHGHEH HDHGHGHHEH EHDHGHDHHH HDHGHDHGHD HGQDHGDHCG PDCGHDHHHH
DANRHDDHIR AFCMVIDRPV PWNGFVDFME ALIAQAGENL LRVKGLLNVQ ESELPVVVHG
VQHMFHPPVR LEDWPSEDHR TKLVFITRDV GQTVIEPLFN GLVWGEGK
//
