ID H1G5D9_9GAMM Unreviewed; 430 AA.
AC H1G5D9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Ribulose-bisphosphate carboxylase {ECO:0000313|EMBL:EHQ53026.1};
GN ORFNames=ECTPHS_10074 {ECO:0000313|EMBL:EHQ53026.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ53026.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ53026.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ53026.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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:EHQ53026.1}.
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; AGBG01000022; EHQ53026.1; -; Genomic_DNA.
DR RefSeq; WP_008932593.1; NZ_AGBG01000022.1.
DR AlphaFoldDB; H1G5D9; -.
DR STRING; 519989.ECTPHS_10074; -.
DR PATRIC; fig|519989.5.peg.1986; -.
DR eggNOG; COG1850; Bacteria.
DR OrthoDB; 9770811at2; -.
DR Proteomes; UP000005314; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
PE 4: Predicted;
FT DOMAIN 151..429
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
SQ SEQUENCE 430 AA; 47464 MW; BAD5FC95C0F01468 CRC64;
MQPADIEGFF ADPADLDLNR YLILDYELEC VGDPRLAVAH LCSEQSTAQW KRVDVDEDLR
PRFAAKVIEM EILEEREALS YPVTHAAEGR IFACRVRIAH PHENFGPRIP NLLSAVCGEG
PFFTPGIPLI KLMDIHFPEV FLRAFQGPKF GVQGLRELLH AHDRPIFLGV IKPNIGLPPE
AFSAIASEAW LGGLDIAKDD EMLADPDWSP LDERCRHLGE ARRRAEQETG TPKMYMANIT
DEVDRLTELH DIAVARGANA LLVNAMPVGL SAVRMLRKHT QVPLFGHFPF IAAFSRLPHY
GIHSRVITRL QRLAGYDSVI MPGFGPRMMT SDEEVMANVR ACLEDIGPIK PCLPVPGGSD
SAATLQRVYE KVGSVDFGFV PGRGVFGHAM GPRGGAASIR QAWDALARGV PVPEQARQHP
ELAAALKQFQ
//