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Database: UniProt/TrEMBL
Entry: A0A1L7AKZ2_9PROT
LinkDB: A0A1L7AKZ2_9PROT
Original site: A0A1L7AKZ2_9PROT 
ID   A0A1L7AKZ2_9PROT        Unreviewed;       396 AA.
AC   A0A1L7AKZ2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-SEP-2017, entry version 5.
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=RGI145_17215 {ECO:0000313|EMBL:APT59445.1};
OS   Roseomonas gilardii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Roseomonas.
OX   NCBI_TaxID=257708 {ECO:0000313|EMBL:APT59445.1, ECO:0000313|Proteomes:UP000185494};
RN   [1] {ECO:0000313|EMBL:APT59445.1, ECO:0000313|Proteomes:UP000185494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U14-5 {ECO:0000313|EMBL:APT59445.1,
RC   ECO:0000313|Proteomes:UP000185494};
RA   Fomenkov A., Akimov V.N., Vasilyeva L.V., Andersen D., Vincze T.,
RA   Roberts R.J.;
RT   "Complete Genome and Methylome Analysis of Psychrotrophic Bacterial
RT   Isolates from Antarctic Lake Untersee.";
RL   Submitted (MAY-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; CP015583; APT59445.1; -; Genomic_DNA.
DR   RefSeq; WP_075800162.1; NZ_CP015583.1.
DR   KEGG; rgi:RGI145_17215; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000185494; Chromosome 1.
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:UP000185494};
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}.
FT   DOMAIN      250    376       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     45     45       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    271    271       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     319    319       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      45     45       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   396 AA;  42188 MW;  90E6A3FCA8FB159F CRC64;
     MHSPARERLW PAAGAILTID LGAIRANWRW LRDRVAPAAC GAVLKADAYG LGAALVGPAL
     LAEGCRDFFV AHLEEGIALR QDLRGQPGAE EARIHVMHGL FDGTEREALA HGLIPVLNSL
     EQVAGWAGLS RAEGRRLPAW LQLDTGMARF GFSVGELDRL LEDGRDLAAV EPIRVMSHLA
     CADEPGHPAN AAQLGAFNAM RRRLPHLPTS LAASSGIFLD RAWHGDLVRP GVALHGVAPL
     PRGENPLRPV LRLDARVVQT RSVPAGTAVG YGHSFTTRTP SRLATIAVGY ADGFLRSASN
     RGRAMWKGMP MPILGRVSMD SIVLDASALP ENALRPGDTV ELIGPDHDLE AVAEAAGTIP
     YEILTSLGQR YHRRYETGAP GSSGEVLQPT GPAVTA
//
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