ID C6HX38_9BACT Unreviewed; 416 AA.
AC C6HX38;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Succinyl-CoA synthetase, beta subunit {ECO:0000313|EMBL:EES52748.1};
GN ORFNames=UBAL3_92050120 {ECO:0000313|EMBL:EES52748.1};
OS Leptospirillum ferrodiazotrophum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=412449 {ECO:0000313|EMBL:EES52748.1, ECO:0000313|Proteomes:UP000009374};
RN [1] {ECO:0000313|EMBL:EES52748.1, ECO:0000313|Proteomes:UP000009374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19429552; DOI=10.1128/AEM.02943-08;
RA Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M.,
RA Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J.,
RA Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., Banfield J.F.;
RT "Community genomic and proteomic analyses of chemoautotrophic iron-
RT oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum
RT ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.";
RL Appl. Environ. Microbiol. 75:4599-4615(2009).
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DR EMBL; GG693873; EES52748.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HX38; -.
DR Proteomes; UP000009374; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000009374};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..217
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 416 AA; 45561 MW; 072023439D661F5B CRC64;
MKLYEHEALG AIFKKYKIPV PRYIFATDMN DAVNQFVEKE PGVVVKSMVL VGKRGKAGAV
KVVSDKAKVP DVVRDLATRE VYGEKSIGAL VEEKLDIEKE FYLSVTYSTK DRAPAIIFSE
HGGMDVEEID PKLIHTHVIS DVRSVYPYQI RQFLTGIGFS DKDLLRPLSE VIVNVYHAFV
GAECRLLEIN PLVVARSGDK RKIVAADAVV ILDDDASVNP AVVYGARSAQ GRPMTQREQD
AILIDQGDHR GKAGSYVELE GDIAMMTFGG GGSTVTAETA IEAGLRIANL TDIGGNPPAE
KMYRISRIIL SKPGIKGVLV CGGTASNTRI DVTLGEGLAK ALDDMNAEGK LDKNLIWVVR
RSGPEYVKGL KMLHECFVRN GIRGEIYDSQ LPITEAPIRL KELLIKHAGY KPEQIV
//
