ID A0A0D8HIC2_9ACTN Unreviewed; 711 AA.
AC A0A0D8HIC2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE SubName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000313|EMBL:KJF17673.1};
GN ORFNames=AXFE_14680 {ECO:0000313|EMBL:KJF17673.1};
OS Acidithrix ferrooxidans.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidithrix.
OX NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF17673.1, ECO:0000313|Proteomes:UP000032360};
RN [1] {ECO:0000313|EMBL:KJF17673.1, ECO:0000313|Proteomes:UP000032360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Py-F3 {ECO:0000313|EMBL:KJF17673.1,
RC ECO:0000313|Proteomes:UP000032360};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT strain Py-F3.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJF17673.1}.
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DR EMBL; JXYS01000032; KJF17673.1; -; Genomic_DNA.
DR RefSeq; WP_052605205.1; NZ_JXYS01000032.1.
DR AlphaFoldDB; A0A0D8HIC2; -.
DR STRING; 1280514.AXFE_14680; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000032360; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000032360}.
FT DOMAIN 497..533
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 711 AA; 75581 MW; 95E3A4FEDC728F85 CRC64;
MDRTALDALF SPRSIAIVGA SNDPKRIGGR PLNATIKAGF EGPIYPINPN YDEVLGRKSY
PRLSDLPEAV DLVVVAVGSR YVESVIEDAA MAGARSLVVF SSGYSELGPD GRIAQDRIAS
LCQSNQMAML GPNCLGVINQ KAKAMASFTA ALDLDLIKGG NIGFACQSGA FGSYFLTLVS
RRGLGINLWV ATGNEAQVSV ADAIEYMADL DEISVIGGYI EGVQDCDRLR SALIKAHDAK
KPVVLMKAGV TEAGARAAIS HTGSMAGDDQ VFSAFVEHYG GYRVSDLDEM IDLIQGISLG
AYPKGKNLCL LTMSGGAGIL MADAAGEADL ALPSPSPEVK DHLSALVPYA ALDNPVDFTG
QFINDPTLGG QFLTKLSDSN LYDAFVTFVG HTALDETIAT PVLETISTLS TQGGAPHFLV
GLTTPPLEKL LLQAKVPFLT NPAKAVKLVR SLYEVSETLA RPIESLAWQG DPHIEALFDL
LVASQAGAEV VPEVASLSFF RSCGISTVMA IRATSPQEAL KAAQEIGFPI VLKIDSPQVP
HKAKVGGVML SINSKRELEH ACYEMMGKVA RRVSGAEIRG FVVEPMVSEG LEVILGVRRD
RDYGCVIMVG SGGVMAETSS DIQIRLAPIT LQGAISAIER TEFGKAIRSG VLARDYDFEG
LAQLMVTLSK IVVSNKRISE IDLNPVLFRQ RDKDPIVLDA LVVLAPEKVP S
//
