ID Q8RR27_SPHPI Unreviewed; 709 AA.
AC Q8RR27;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Feruloyl-CoA synthetase {ECO:0000313|EMBL:BAB86294.1};
GN Name=ferA {ECO:0000313|EMBL:BAB86294.1};
OS Sphingomonas paucimobilis (Pseudomonas paucimobilis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=13689 {ECO:0000313|EMBL:BAB86294.1};
RN [1] {ECO:0000313|EMBL:BAB86294.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SYK-6 {ECO:0000313|EMBL:BAC79255.1};
RX PubMed=12200295; DOI=10.1128/AEM.68.9.4416-4424.2002;
RA Masai E., Harada K., Peng X., Kitayama H., Katayama Y., Fukuda M.;
RT "Cloning and characterization of the ferulic acid catabolic genes of
RT Sphingomonas paucimobilis SYK-6.";
RL Appl. Environ. Microbiol. 68:4416-4424(2002).
RN [2] {ECO:0000313|EMBL:BAC79255.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SYK-6 {ECO:0000313|EMBL:BAC79255.1};
RX PubMed=15090517; DOI=10.1128/JB.186.9.2757-2765.2004;
RA Masai E., Sasaki M., Minakawa Y., Abe T., Sonoki T., Miyauchi K.,
RA Katayama Y., Fukuda M.;
RT "A novel tetrahydrofolate-dependent O-demethylase gene is essential for
RT growth of Sphingomonas paucimobilis SYK-6 with syringate.";
RL J. Bacteriol. 186:2757-2765(2004).
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DR EMBL; AB072376; BAB86294.1; -; Genomic_DNA.
DR EMBL; AB110975; BAC79255.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RR27; -.
DR SMR; Q8RR27; -.
DR BioCyc; MetaCyc:MONOMER-15132; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 501..552
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 709 AA; 73863 MW; 926F8D1417394BEA CRC64;
MTVEAGVRPQ AGARDINRLL RPRSIAIVGA SETPGSLGAS VLANLVRNEF PGDIHLVNPK
RETISGRPAV PSVDALPEGV DCAILAIPRV AVLDTMRQLA ARKAGAAIIF AAGFAEGGEQ
GMADQQEIGR IAHEAGIVVE GPNCLGSVNY LDRIPLTFID TDIKAPSPGG VGIVSQSGAM
AAVLAVMLES RTLDLTYSVS TGNEAGSGVE DYVEFMIADE KTRIIAMIVE QFRDPARFLA
LMDKANAAGK LVVLLHPGKS SAARESAATH TGAMAGDYKL MRAKVERAGV VVAETLEELG
DITEIAARCP ALPSGGTAVL GESGALKALT LDLAEELELA LPTLDDGNAP ALRAALPEFV
PVSNPLDLTA QGLVDPDMYY RTLAALFEDD RVGTIFAGII QTNPATIGIK LPPFLKAVRE
LKATKPVIFG GVDEGADVPA DWIEQLRAEG IPYFPTTERA LRAIRRLSAA GARDASRTDA
APASVPALAS EKGVVPEYKA KALLAPLGIS FPKGQFAATV EDAIAAAEAI GGPVVMKAQA
AALSHKSDAG GVALNLVGAE AIRAAWDKMF ADVKRYDASI ILDGVLIEAM GARGLELIVG
AKNDPQWGPV ILAGFGGVTA EILQDVRLLS PDMTKEAIVA ELGKLKQAAL LHGYRGSPAL
DVGAVAELIG QVGRLLRGEP RIQELDLNPV VVYPEGQGAI ALDALMLVD
//
