ID   ALR_PENMO               Reviewed;         120 AA.
AC   P83944;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Alanine racemase;
DE            EC=5.1.1.1;
DE   Flags: Fragments;
OS   Penaeus monodon (Giant tiger prawn).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6687;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CHARACTERIZATION, AND SUBUNIT.
RC   TISSUE=Muscle {ECO:0000269|PubMed:12431412};
RX   PubMed=12431412; DOI=10.1016/s1096-4959(02)00187-2;
RA   Yoshikawa N., Dhomae N., Takio K., Abe H.;
RT   "Purification, properties, and partial amino acid sequences of alanine
RT   racemase from the muscle of the black tiger prawn Penaeus monodon.";
RL   Comp. Biochem. Physiol. 133B:445-453(2002).
CC   -!- FUNCTION: Highly specific to D- and L-alanine and does not catalyze the
CC       racemization of other amino acids.
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:0000269|PubMed:12431412};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5 in the direction of L to D, and 10 for the reverse
CC         direction.;
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius for both directions.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12431412}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P83944; -.
DR   SMR; P83944; -.
DR   GO; GO:0008784; F:alanine racemase activity; IDA:UniProtKB.
DR   GO; GO:0018366; P:chiral amino acid racemization; IDA:UniProtKB.
DR   Gene3D; 2.40.37.10; -; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..120
FT                   /note="Alanine racemase"
FT                   /id="PRO_0000114609"
FT   ACT_SITE        24
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000250|UniProtKB:P10724"
FT   NON_CONS        51..52
FT                   /evidence="ECO:0000303|PubMed:12431412"
FT   NON_CONS        74..75
FT                   /evidence="ECO:0000303|PubMed:12431412"
SQ   SEQUENCE   120 AA;  13356 MW;  13B20BEF8F5108BD CRC64;
     QPAFSVVTRP TFYKLLKAGR DIGYDGTYTT SEDEWIANFT TGWSDQLSRR LSTRLPRLYT
     RNGKIVRICP SLEYLFLEAS EPFTSRGITR HVAATTGCVQ DLGTDLDFIR PGGAITGLCS