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ALR1_CALS4
ID   ALR1_CALS4              Reviewed;         388 AA.
AC   Q8RAK6;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr1; OrderedLocusNames=TTE1207;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; AE008691; AAM24437.1; -; Genomic_DNA.
DR   RefSeq; WP_011025537.1; NC_003869.1.
DR   PDB; 4Y2W; X-ray; 2.70 A; A/B=1-388.
DR   PDBsum; 4Y2W; -.
DR   AlphaFoldDB; Q8RAK6; -.
DR   SMR; Q8RAK6; -.
DR   STRING; 273068.TTE1207; -.
DR   PRIDE; Q8RAK6; -.
DR   EnsemblBacteria; AAM24437; AAM24437; TTE1207.
DR   KEGG; tte:TTE1207; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_9; -.
DR   OMA; ELMAVQH; -.
DR   OrthoDB; 859043at2; -.
DR   BRENDA; 5.1.1.1; 6784.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000555; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..388
FT                   /note="Alanine racemase 1"
FT                   /id="PRO_0000114588"
FT   ACT_SITE        40
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        268
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   STRAND          8..14
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           15..28
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           48..58
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           68..76
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           109..121
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           144..155
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   TURN            172..175
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           177..195
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   TURN            196..198
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          202..208
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           209..214
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           216..219
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          278..284
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           287..289
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           293..295
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          300..303
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          306..312
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          319..322
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          334..340
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           348..354
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   HELIX           359..365
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          372..376
FT                   /evidence="ECO:0007829|PDB:4Y2W"
FT   STRAND          379..384
FT                   /evidence="ECO:0007829|PDB:4Y2W"
SQ   SEQUENCE   388 AA;  44126 MW;  8D8E10CF5E20DC9E CRC64;
     MKFDGVRPTR VEVYLDAITH NFREIKKIVG KNVKIMAVIK GDAYGHGASY VAKFLEKEGV
     DYFGVATTEE ALELREKGIK TPILIFGYTP PTQLRQIVKH DLTQTVYDIK YAKELEKESL
     KQNKRAKVHI KIDTGLGRIG YIDFDLAQKE ILEMANMRGL ILEGIYSHFA AASEDDRDYC
     KEQFDKFMNL ISSLEKKRLK IPLKHIANAA AILNLNYSHL DMVRPGIILF GAYPSKRVER
     KVELRETLRF TTRVVHLKDV PAGFFIGYGK SFVTKRKSVI ATIPVGYADG LDRRLSNNYK
     LLLKGKYVPI VGRVCMDQCM IDVTDVEGVE IGDEVVIIGT QNNETVSVES MADKIETIPQ
     EVFSRISRRV PRVYFYDGIK IGEVNYLK
 
 
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