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Database: UniProt/TrEMBL
Entry: A0A168YBY3_9PROT
LinkDB: A0A168YBY3_9PROT
Original site: A0A168YBY3_9PROT 
ID   A0A168YBY3_9PROT        Unreviewed;       376 AA.
AC   A0A168YBY3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 11.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=A6A40_13890 {ECO:0000313|EMBL:ANC92877.1};
OS   Azospirillum humicireducens.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC92877.1, ECO:0000313|Proteomes:UP000077405};
RN   [1] {ECO:0000313|EMBL:ANC92877.1, ECO:0000313|Proteomes:UP000077405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC92877.1,
RC   ECO:0000313|Proteomes:UP000077405};
RX   PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA   Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT   "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium
RT   isolated from a microbial fuel cell.";
RL   Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP015285; ANC92877.1; -; Genomic_DNA.
DR   EnsemblBacteria; ANC92877; ANC92877; A6A40_13890.
DR   KEGG; ahu:A6A40_13890; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000077405; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077405};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077405}.
FT   DOMAIN      247    373       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     44     44       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      44     44       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  39851 MW;  6595A14A8ADF8BA1 CRC64;
     MTRVTSDQTP RAGAILTVDV GAVVANWTQL RDRVAPAECS AVVKADAYGL GAARVVPALA
     AAGCRTFVVA QLEEALAVRR ALEPVAPEAQ VFSLGGLPPG YEGEFIAGRI LPVLNHLGEI
     AAWRAFTASR GEVLPAVIHI DTGMNRLGLG PDELDELAGH PDWLEGINVR YWMTHLACAD
     EFDNPMTGEQ LERFRSALAR LPKAKASFAN SSGIFHGADH HFDLARPGCA LYGVNPTPHL
     PNPMRGTVRL DARLLQVRNC SAPMTVGYGA AHKVTGPARI ATIGVGYADG YLRSLSGKGH
     VFVDGVAAPI VGRISMDLIT IDVTGLPENV AQAGRMVELI GPSRPVDTVA AEAGTIGYEV
     LTSLGQRYHR VYVSGE
//
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