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Database: UniProt/TrEMBL
Entry: A0A161HPY2_9MICO
LinkDB: A0A161HPY2_9MICO
Original site: A0A161HPY2_9MICO 
ID   A0A161HPY2_9MICO        Unreviewed;       403 AA.
AC   A0A161HPY2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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:ANC31142.1};
GN   ORFNames=I598_1589 {ECO:0000313|EMBL:ANC31142.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae;
OC   Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC31142.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC31142.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC31142.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014209; ANC31142.1; -; Genomic_DNA.
DR   EnsemblBacteria; ANC31142; ANC31142; I598_1589.
DR   KEGG; ido:I598_1589; -.
DR   PATRIC; fig|1300344.3.peg.1596; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000076794; 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:UP000076794};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ANC31142.1};
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:UP000076794}.
FT   DOMAIN      255    397       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     42     42       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    276    276       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     142    142       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     333    333       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      42     42       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   403 AA;  40958 MW;  F49F91C150A91F5B CRC64;
     MTIPPFAAGT TARAVVDLAA VTHNVRALRG HAPTAAVMAV VKADGYGHGM LPVARAALAG
     GASWLGVATA EEALALRAGL RDVDVPLLVW LLAPGAPFAA LVAADVDVTV AAPWSVDEVA
     AGARAAGRPA RVHVKVDTGL SRNGVAPAAL PDVARRLADL EAAGTVQVVG LMSHLAAADE
     PGHPSVDRQA TAFAAATDVL HEAGLRPSVR HLANSAATLT RPDLHLDLVR PGISVYGFSP
     GPLLGTPGDF GLRPAMTLQA RLAQVKDVPA GEGVSYGHLY TTPRDTRVGL VPLGYGDGIP
     RHASGGTAGP GGPVAVGSGD AARVLRVVGR VCMDQMVLDL GPDAVEREGD VVTLFGASDG
     VADGATVPNA QDWADAAGTI SYEIVTRLGA RVPRVHVHEG DHE
//
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