ID T1DWA9_9HELI Unreviewed; 340 AA.
AC T1DWA9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Alanine racemase {ECO:0000313|EMBL:GAD19448.1};
DE EC=5.1.1.1 {ECO:0000313|EMBL:GAD19448.1};
GN ORFNames=HFN_0579 {ECO:0000313|EMBL:GAD19448.1};
OS Helicobacter fennelliae MRY12-0050.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1325130 {ECO:0000313|EMBL:GAD19448.1, ECO:0000313|Proteomes:UP000018143};
RN [1] {ECO:0000313|EMBL:GAD19448.1, ECO:0000313|Proteomes:UP000018143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRY12-0050 {ECO:0000313|EMBL:GAD19448.1,
RC ECO:0000313|Proteomes:UP000018143};
RA Rimbara E., Matsui M., Mori S., Suzuki S., Suzuki M., Kim H., Sekizuka T.,
RA Kuroda M., Shibayama K.;
RT "Draft Genome Sequence of Helicobacter fennelliae Strain MRY12-0050,
RT Isolated from a Bacteremia Patient.";
RL Genome Announc. 1:e00512-13(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
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:GAD19448.1}.
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DR EMBL; BASD01000019; GAD19448.1; -; Genomic_DNA.
DR RefSeq; WP_023948727.1; NZ_BASD01000019.1.
DR AlphaFoldDB; T1DWA9; -.
DR STRING; 1325130.HFN_0579; -.
DR eggNOG; COG0787; Bacteria.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000018143; Unassembled WGS sequence.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:GAD19448.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000018143}.
FT DOMAIN 227..340
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT MOD_RES 33
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 340 AA; 37694 MW; D3C0327D10690937 CRC64;
MAEIILDSAR FIHNLDCIAH HIKSRQKLAL VLKDNAYGHG LVEIAQMAKT YGICNVFVKS
YAEALKIKDL FSSISVLYGG VPDSCPDNIY CSIASLSQLQ SLHSHCNIEL KVNIGMNRNG
IELSELDSAL RIIIERSLRL VGVFGHNGYG DNDDETFFTS QSTFSHIKQK VSTFCATHNL
SQPRFHSLST SGTLRSKHIT DDLVRIGIGA YGYHTSEIPL DVEFKPIASL WADRISSQHL
KKGDKIGYGG VSVVQKEGIF STYDVGYGDG LPRLARGFGK LFCASGEEIL PIMSMDCFSC
ESQKDRICVF DDVTGFARVF RTIPYVILTH LSPFLKRVVI
//
