ID   D3HJG6_LEGLN            Unreviewed;       861 AA.
AC   D3HJG6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Putative alanine racemase {ECO:0000313|EMBL:CBJ12558.1};
DE            EC=5.1.1.1 {ECO:0000313|EMBL:CBJ12558.1};
GN   OrderedLocusNames=LLO_2162 {ECO:0000313|EMBL:CBJ12558.1};
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ12558.1, ECO:0000313|Proteomes:UP000001060};
RN   [1] {ECO:0000313|EMBL:CBJ12558.1, ECO:0000313|Proteomes:UP000001060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150 {ECO:0000313|EMBL:CBJ12558.1,
RC   ECO:0000313|Proteomes:UP000001060};
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600821-50};
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DR   EMBL; FN650140; CBJ12558.1; -; Genomic_DNA.
DR   RefSeq; WP_012979258.1; NC_013861.1.
DR   AlphaFoldDB; D3HJG6; -.
DR   STRING; 661367.LLO_2162; -.
DR   KEGG; llo:LLO_2162; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_332278_0_0_6; -.
DR   OrthoDB; 9813814at2; -.
DR   Proteomes; UP000001060; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR036188; FAD/NAD-bd_sf.
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; SSF51905; FAD/NAD(P)-binding domain; 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:CBJ12558.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR600821-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          725..859
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   BINDING         593
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         801
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         487
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   861 AA;  98233 MW;  4B45273094D56147 CRC64;
     MYSSKISTDS MRNYIIMGGG PVGCYLAYAL LKQKNARVFI LEGRTFERPQ VIRIPYCIAK
     NLPEYVKNIM WADEKTRLRI FNTYQAEDES FWPKPGYPYW PWINIGLFQE SMINFLQNST
     EFKNRFFFIS VYFDLEKINY QSQIKKILSA NHPQIIENIT AIYCTCGTYA KSLRSELNLL
     DGKISEPKGH GVYLIYQNKG IENYLRNSNP ILYSKLGENG ISYAASNNCN YDVQLYTYPS
     GELSSVLNEI PEDFIQCVKY NSISNRFDMT GSGLSENSKQ WFEVYKKIII NETNKHGIEL
     PSDLEKIQIF YASRSEYYWN RAAIKVLWQK NHVPIFFLGD SAGSTDYKFG LSVGRGFLAV
     DMLINSMQYY HYDFDKIAAN YQAYWNRIIL SEFNKGPLLP LEPWIQYQYL IKGREVGFQN
     NKFIHYIDNE QYEIYLDEYQ NLSTDFSKTS EKSAILFINT KAIKENIKNI ISFGKQCSHS
     KIIGVIKSNG YGLGSKLVSD LAIEAGIDFL AVAKLQEAIA LRNSGIPSTV RLMTFEAPMI
     YDLSTYAANQ IEVIIPSSKN AASINMIAKW LQNKHRVLGK LKVHIMVDTG LRRDGGYESN
     IPDSVMETIS KLQLLDPNQV EFAGLSTHLA CYRCTDYNGD EIINFRALQF HRFEKVIKFL
     FSQGVQIPLI HIGGGLALLA EKWPLQFEKF LKEFNVGFYT RVGHGLYGME LEKDLHLDSP
     RLRQVVKMDL QVRNVFYVEE GEPVSYGGYC RAPKDGAWIA TLAGGWAEGV PRTAQTLGEW
     QHGMMVCINN HQYPIVGKIN MNAMMVNLGS LTKVKPGDRA IIFGWSDHEP KLNDLAQLSG
     QIAPSIMVNV PTSMPRVAVS E
//