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Database: UniProt
Entry: A0A166PYK0_9RHOB
LinkDB: A0A166PYK0_9RHOB
Original site: A0A166PYK0_9RHOB 
ID   A0A166PYK0_9RHOB        Unreviewed;       699 AA.
AC   A0A166PYK0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=CoA-binding protein {ECO:0000313|EMBL:KZX93861.1};
GN   ORFNames=A3721_11115 {ECO:0000313|EMBL:KZX93861.1};
OS   Sulfitobacter sp. HI0023.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZX93861.1, ECO:0000313|Proteomes:UP000077323};
RN   [1] {ECO:0000313|EMBL:KZX93861.1, ECO:0000313|Proteomes:UP000077323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0023 {ECO:0000313|EMBL:KZX93861.1,
RC   ECO:0000313|Proteomes:UP000077323};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-2016) 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:KZX93861.1}.
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DR   EMBL; LWEQ01000647; KZX93861.1; -; Genomic_DNA.
DR   RefSeq; WP_067920398.1; NZ_LWEQ01000647.1.
DR   AlphaFoldDB; A0A166PYK0; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000077323; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000077323};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          485..521
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   699 AA;  73521 MW;  39117509D02C3D15 CRC64;
     MDAIFKPRSV AVIGASSDPK RIGGRPVDFL KRHGFDGPIL PINPKSPEVQ GLTAYPSISE
     APTTPDLAVI ALPAPLAVQA VEQCAAQGVR GAVIFSSGFS EVDADGAALQ ARMVDIAREG
     GMRLVGPNCL GIANVRHNLY ATFTPGVEKH LPKPGGVSIV SQSGAFGSYC MTLVRMRGLG
     VNIWATTGNS CDVDFADAVA YCAQDDDTRV IMGYLEGATD RDRLVEALEL ARACEKPVVM
     MKVGRSAVGA EAAQSHTASL AGADAVYDAA FRQYGVYRAQ SVDEMFDVTY ACAESAAMMQ
     GDRLGLVTVS GGVGVLMADE AEKLKLDVPA LPDHAQKKLK EVLPFAGVRN PVDVTAQLVN
     QIDLLETNMD VLFGDGDIDG AIIFMSTVGL VADLNEAIRS GLERIRAKYP GRPMLFCSLT
     EPEGRAAYEK SGFIVFEEPT RAVRAMAALR YFARSFARAG EKDPIPELSN LSPLPDGMVN
     EIEAKALLAE AGIGIVRETL ATTPEAAAQA AQEMGFPVVL KIASPDILHK SDIGGVALDL
     HSAEDVRSAG ARILDLASEK MPGARIDGLV VAEQAAPGLE AILGVTQDPA FGPVVMFGLG
     GVFVEALEDV SFRVAPFGPA EARRMIDEIR SRKLLDAFRG APERDLDALA NALARLSAFA
     AHHGAALETI DVNPLIVGAS GQGAVAADGV IIPAMRGDH
//
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