ID B6AQJ3_9BACT Unreviewed; 416 AA.
AC B6AQJ3;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Succinyl-CoA synthetase, beta subunit {ECO:0000313|EMBL:EDZ38636.1};
GN ORFNames=CGL2_11068123 {ECO:0000313|EMBL:EDZ38636.1};
OS Leptospirillum sp. Group II '5-way CG'.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ38636.1};
RN [1] {ECO:0000313|EMBL:EDZ38636.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14961025; DOI=10.1038/nature02340;
RA Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J.,
RA Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., Banfield J.F.;
RT "Community structure and metabolism through reconstruction of microbial
RT genomes from the environment.";
RL Nature 428:37-43(2004).
RN [2] {ECO:0000313|EMBL:EDZ38636.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18651792; DOI=10.1371/journal.pbio.0060177;
RA Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P.,
RA Banfield J.F.;
RT "Population genomic analysis of strain variation in Leptospirillum group II
RT bacteria involved in acid mine drainage formation.";
RL PLoS Biol. 6:E177-E177(2008).
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DR EMBL; DS995261; EDZ38636.1; -; Genomic_DNA.
DR AlphaFoldDB; B6AQJ3; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..217
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 416 AA; 45634 MW; FE0CAEFDA8D08B3F CRC64;
MKLYEHEALE SIYKKYKIPA PRFVFATEPN EKVREFIEKE PAVVIKSMVL VGKRGKAGAV
KVVSDKAQAI DVFKDLASRE VYGEKSIGAL VEEKLDIKKE FYLSVTYSTK DRAPAIIFSE
HGGMDVEEIN PALIHTHVIK DVRSVYPYQI RNFLVGIGFS DPDLLRPLSE LIVNVFHAFW
LTEARLLEIN PLVVAQVGDK KKLVAADAVV LLDDDASVSP AVRYGARGGM GRPLTQREQD
AILIDQGDHR GKAGSYVELD GDVALMTFGG GGSTVTAETA IEAGLRIANL TDIGGNPPAE
KMYKIARIIL SKPGLKAVLV CGGTASNTRI DVTLGEGLAK ALDDMKAEGK LDPNLIWVVR
RSGPEYVKGL KMLHECFVRN GIRGDIYDSQ LPITEAPLRL RELMVKHIGY KPEVIG
//
