ID A0A132BU39_9RHOB Unreviewed; 1358 AA.
AC A0A132BU39;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:KUP91898.1};
DE EC=2.7.9.2 {ECO:0000313|EMBL:KUP91898.1};
GN Name=ppsA {ECO:0000313|EMBL:KUP91898.1};
GN ORFNames=TRIHO_32020 {ECO:0000313|EMBL:KUP91898.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP91898.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP91898.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP91898.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003945}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003945}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family.
CC {ECO:0000256|RuleBase:RU003945}.
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:KUP91898.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LPUY01000082; KUP91898.1; -; Genomic_DNA.
DR PATRIC; fig|1768241.3.peg.3346; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000068382; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
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; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR028055; YidC/Oxa/ALB_C.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF02096; 60KD_IMP; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 2.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Pyruvate {ECO:0000313|EMBL:KUP91898.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068382};
KW Transferase {ECO:0000313|EMBL:KUP91898.1};
KW Transmembrane {ECO:0000256|RuleBase:RU003945, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 175..261
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 293..400
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT COILED 1132..1166
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1358 AA; 147563 MW; 29ACF5704656DBE2 CRC64;
MPGNSFRSEG HLVTTLNTPT CITRSVKIYF CLSVSMTFFL TNAAPALAIP SPELVLGSVS
SLSQILALVV ALLSGFGAMV AGRLGLKPGT FGQRRYPVRL IAGLVAVAAL LAAANHWQWQ
SHKTKELQRL QATLSRPAQF DGTTLKDPKL KETSYTAQET HPQGITTAQA AALLASDDVR
FFDIRETAEH EMGTLPGATH VRFPDFQQSV PVAPGERVVL FCHNGNRSSE TCAELAKMGI
DCSFVAGGIE KWIVESRPFS DAEVQSLSDL RAIPDYENKS RLLSTDAFTK MVQSGPLQIV
DTRYPGNFAA GHLPGAINIP IRAITTEDLR SRIAALEDKP TVVACYDRRS CFMGQVLGLE
LTRAGLPFAG RYTLPWEYFV APPPKPHVSA WLAEQNKTVW TKAVAAIGTA LLWGHERAHL
LVSLFVLALV SRLMVLPIAL KSERDQITLR MHKPELQAVK SRLAADPMRK SRAIQAFYAK
HGLTPMRNLT ALLFLPLMML GLQSAEFAAT AIAEPFLWVA DLGAPDPSYM AALLTSALGG
VYLFSAMARD RRSAVLWLGL GVPLLFVLTM GLSTAGNVYL SISLAGLLLQ HFYVSGKLAR
ATVTLRHMAR LPRGVVTLDN TAQLAQAGNK ALRLSQLANA GFPVPDGIVL TDRYLAQFEQ
AAPQRRQQMA ARLWRQIGPT PCAVRSSASQ EDGADQSFAG VFDSVLDVTG PTLPSAIETV
LASFGSARAQ SYGGTDDTAP RNVAGAGNIL IQHMIEASYA GVLFTQDPQA PGMMLLEWVA
GKGEDLVSGR ATPKTARFGR YSFDAAAHGA EAPFDARALL ALGRRIETLF DAPQDVEWAW
TEGQFYILQS RDITTTTVGS AEDQARAQEW RRLFATVTED NCDPQITLLE QDEMSEVLPR
PTPLSFSLMS QIWAPGGSLD LACRALRLPY TLPEAPNAHL IRLFGKTYVD TRLKQQLTMD
LSGNRAIRLK KQLTPTLDRF AHEVLPALND TVEDWRAIRF EALPRAKILD AISRLKQEFV
TGIYVEAEKI NLLSAFAMKE ATSAAQGDPA LRSHLMQADL HYTPASLLAQ CHGTEEEAQA
MALQRMGHRA MFDYELSTPR YAEAPSLLFS LMEPEVKPLR PSVMPADLPT ELRQLIDTAV
AYQDLKERAK HEAMRLLAEL RRALVALGAE SGLDELVFHL TIEELLQGDW SKPEHLRQIA
DARRSHDALA RKSAPTQTQL SLADCEQLSA GSIGAAADGP MHGTCVAGSG EATGRAFRVA
DEASFGEAAF VGFAPGDIIL CDMVNPAWLP QLQQAGAVVS AVGGWLSHMA IVAREKDILM
LVGATGLDGL EQGETITVTD SGEIRQPQAE GSEQARRA
//
