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Database: UniProt/TrEMBL
Entry: E4NCK1_KITSK
LinkDB: E4NCK1_KITSK
Original site: E4NCK1_KITSK 
ID   E4NCK1_KITSK            Unreviewed;       394 AA.
AC   E4NCK1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   28-FEB-2018, entry version 54.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:BAJ28932.1};
GN   OrderedLocusNames=KSE_31220 {ECO:0000313|EMBL:BAJ28932.1};
OS   Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC
OS   A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ28932.1, ECO:0000313|Proteomes:UP000007076};
RN   [1] {ECO:0000313|EMBL:BAJ28932.1, ECO:0000313|Proteomes:UP000007076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC   KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX   PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA   Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA   Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA   Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T.,
RA   Horinouchi S., Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A.,
RA   Nomoto F., Miura H., Takahashi Y., Fujita N.;
RT   "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT   snapshot of the family Streptomycetaceae.";
RL   DNA Res. 17:393-406(2010).
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; AP010968; BAJ28932.1; -; Genomic_DNA.
DR   RefSeq; WP_014136244.1; NC_016109.1.
DR   ProteinModelPortal; E4NCK1; -.
DR   STRING; 452652.KSE_31220; -.
DR   EnsemblBacteria; BAJ28932; BAJ28932; KSE_31220.
DR   KEGG; ksk:KSE_31220; -.
DR   PATRIC; fig|452652.3.peg.3134; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; KSET452652:G1H62-3167-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007076; 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; -; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007076};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:BAJ28932.1};
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:UP000007076}.
FT   DOMAIN      262    389       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   COILED       17     37       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     48     48       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    283    283       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     149    149       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     331    331       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      48     48       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   394 AA;  41189 MW;  5CFB4BE7ED533D39 CRC64;
     MTTANTTGTP ALAQGARAEA TVDLAALRDN LAALRARTSG AELMAVVKAD AYGHGALRCA
     REAVAAGAGW LGTATPEEAL ALRAAGIGPE QARILCWLWT PGGPWARALR ESVDISISGQ
     WALDELLAAV RETGVPARVH LKADTGLGRN GCQPHDWPDL VENAVKAQAA GLLRVVGVWS
     HFAAADEPGH PSIQAQLDSF AQALAFAERT GVDPEVRHLA NSPATLLLPQ SHYDLVRPGL
     AMYGLSPVPD VGAPADFGLR PVMSLAARLA LVKRVPGGHG ISYGHHYTTS GPTTLGLVPL
     GYADGVPRHA SNTGPVQIGS SWYRVAGRVA MDQFVVDLGG DLPDVGEEVL LFGSGERGEP
     TAEDWARACG TIAYEIITRI GGRVPRRYVG GSRG
//
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