ID S6HRQ1_9GAMM Unreviewed; 303 AA.
AC S6HRQ1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Pyruvate carboxyltransferase domain-containing protein {ECO:0000259|PROSITE:PS50991};
GN ORFNames=OFPI_02080 {ECO:0000313|EMBL:EPJ55908.1};
OS Osedax symbiont Rs2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ55908.1, ECO:0000313|Proteomes:UP000014830};
RN [1] {ECO:0000313|EMBL:EPJ55908.1, ECO:0000313|Proteomes:UP000014830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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:EPJ55908.1}.
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DR EMBL; ASZI01000010; EPJ55908.1; -; Genomic_DNA.
DR AlphaFoldDB; S6HRQ1; -.
DR PATRIC; fig|1330035.3.peg.195; -.
DR Proteomes; UP000014830; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014830}.
FT DOMAIN 5..279
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 303 AA; 32805 MW; B15B9CB9B056C0E5 CRC64;
MSAAVTLIEV SPRDGFQSVV PIIPVADKVA IIRALSQAGL KHIEVGAFVH PKAIPQMADI
NQLLVELRRG DDNCDSFESI VLVPNQRGAV LAAQQQCQRV NFVFSVSEAH NLKNVRKSVD
QSLQELRAVQ QVIEKNPQMQ LRVSLATSFD CPFAGAVDPQ RCLDVLAQVT DICVNVQIAL
CDTTGRAHPF KVEQLFSKAF EQLDNSHQVI FHCHDTYGMA IANVAAAYRS GVRFFDTAVA
GFGGCPFAPG ASGNVATEDV VYFFESAGIS TGIDSEKLRL AIQLAEKIEG AQLGGAIRLL
NRN
//