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Database: UniProt
Entry: A0A0C4YSS2_9BURK
LinkDB: A0A0C4YSS2_9BURK
Original site: A0A0C4YSS2_9BURK 
ID   A0A0C4YSS2_9BURK        Unreviewed;       706 AA.
AC   A0A0C4YSS2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Acetyl-CoA synthetase (ADP-forming) alpha and beta chains, putative {ECO:0000313|EMBL:AJG24984.1};
GN   ORFNames=RR42_s3408 {ECO:0000313|EMBL:AJG24984.1};
OS   Cupriavidus basilensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG24984.1, ECO:0000313|Proteomes:UP000031843};
RN   [1] {ECO:0000313|EMBL:AJG24984.1, ECO:0000313|Proteomes:UP000031843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:AJG24984.1};
RX   PubMed=25977418;
RA   Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA   Chakraborty R., Arkin A.P., Deutschbauer A.;
RT   "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT   Oak Ridge Field Research Center Site.";
RL   Genome Announc. 3:0-0(2015).
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DR   EMBL; CP010537; AJG24984.1; -; Genomic_DNA.
DR   RefSeq; WP_043357367.1; NZ_CP010537.1.
DR   AlphaFoldDB; A0A0C4YSS2; -.
DR   STRING; 68895.RR42_s3408; -.
DR   KEGG; cbw:RR42_s3408; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000031843; Chromosome secondary.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT   DOMAIN          8..103
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   706 AA;  72045 MW;  0B4361128E8393F2 CRC64;
     MNQTLQALLA PRSIAVIGAS DHIHKIGGRP IYYMREHGYA GKLFPVNPQR DTIQGLPAFA
     SLDALPEVPE LAIIVVGGDA AVSAVRDCAR LGVAAAIVIA SGFGEAGEQG RRQQDEMVRV
     ATGAGLRLVG PNSQGLANFG TGTIASFSTM FIEVPPQDGP VAVVSQSGGV SAMVYGLLRG
     QGIGVRHMHA TGNEADITVS ELALAVAHDP DVQLILLYLE SLTDPAVLAQ AAAVARRRGV
     PIVAVKAGRS SAGQRAAASH TGAMANEDRA VGAFLARHGI CRVDDAHALA RCAPLYLRGW
     QASGRQLVVV SNSGASCVMA ADAAEPLGLA LAPLSQATQA ALAQRLPGFA STANPVDVTA
     ALLTNSGLFG DVLPLVAADP AADLLLLDIP VAGMGYDLPR FARDAASFAD SAGKPIAVAA
     WQAPVAAAFR AANVPTYASG AEALAAFAQL VTHQQQLRDV AAQDTAVGAH RPAASDAAGA
     ASSAAGHTLS EAQSLARLAL AGIPVVAHKL CQSVDEAVAA WRELKGPVAV KASSPQVPHK
     SEHGLVALNC NDEHAVAQAF LTQTDILDKL GATCEGVVVA RMERGQRECM VGAHWDPVFG
     PVVLVGDGGK YVEVLRDTAV LLAPCSEAAV ARAVAGLRIA PLLAGVRGEP AVDVAALCRI
     AVRVGQMMLE ADGAIRSIDL NPVMVSAGGA VVVDALMEVA AHAAPA
//
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