ID   B0TMM4_SHEHH            Unreviewed;       406 AA.
AC   B0TMM4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Alanine racemase {ECO:0000313|EMBL:ABZ77384.1};
DE            EC=5.1.1.1 {ECO:0000313|EMBL:ABZ77384.1};
GN   OrderedLocusNames=Shal_2833 {ECO:0000313|EMBL:ABZ77384.1};
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ77384.1, ECO:0000313|Proteomes:UP000001317};
RN   [1] {ECO:0000313|EMBL:ABZ77384.1, ECO:0000313|Proteomes:UP000001317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ77384.1,
RC   ECO:0000313|Proteomes:UP000001317};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC       {ECO:0000256|ARBA:ARBA00023456}.
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DR   EMBL; CP000931; ABZ77384.1; -; Genomic_DNA.
DR   RefSeq; WP_012277911.1; NC_010334.1.
DR   AlphaFoldDB; B0TMM4; -.
DR   STRING; 458817.Shal_2833; -.
DR   KEGG; shl:Shal_2833; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_6; -.
DR   OrthoDB; 9813814at2; -.
DR   Proteomes; UP000001317; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR   CDD; cd06826; PLPDE_III_AR2; 1.
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   InterPro; IPR043698; Racemase_Bsr/Lyr.
DR   NCBIfam; TIGR00492; alr; 1.
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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABZ77384.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR600821-50};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..406
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002753838"
FT   DOMAIN          277..405
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         73
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   406 AA;  43841 MW;  C4D83068A2A3029E CRC64;
     MKTKYTIIAM FVASIGSFST VAAPFLPSDG VSPVEAVQAA NSWLEVNLTQ FDSNIKELKN
     HIQSNVKVCA IMKADAYGNG IAGLMPTVLA NNIPCIGVTS NEEIRIVRDA GFRGSLIRVR
     SASIAEISDT LQYDVEEFVG DANQATLLSA MAAKLDKPLK VHLVLNSGGM GRNGVDVSTQ
     SGLNEAVQIA TTADLDVVGI MTHFPSYDRD DVLVKSKSFY NSALNIIEES GLKRDSVTIH
     SGNSYVALNV PEAHFDMVRP GGVLYGDQPT NPEFPSIVTF KTRIASLVDL PKGATVGYDS
     TIKLERESLL ANLPVGYSDS FPRKMGNTAD VLVNGQRAKV MGVISMNTSM IDVTDLSGVK
     EGDEVVLFGY QGKESILAPE FEKNADVIFP EIYTQWGQTN PRIYVK
//