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Database: UniProt/TrEMBL
Entry: F0M960_PSEPM
LinkDB: F0M960_PSEPM
Original site: F0M960_PSEPM 
ID   F0M960_PSEPM            Unreviewed;       405 AA.
AC   F0M960;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-NOV-2017, 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   OrderedLocusNames=Asphe3_27410 {ECO:0000313|EMBL:ADX73860.1};
OS   Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 /
OS   LMG 23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX73860.1, ECO:0000313|Proteomes:UP000008639};
RN   [1] {ECO:0000313|EMBL:ADX73860.1, ECO:0000313|Proteomes:UP000008639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC   {ECO:0000313|Proteomes:UP000008639};
RX   PubMed=21677849; DOI=10.4056/sigs.1393494;
RA   Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA   Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L.,
RA   Pitluck S., Chen A., Palaniappan K., Markowitz V., Bristow J.,
RA   Velentzas A.D., Perisynakis A., Ouzounis C.C., Kyrpides N.C.,
RA   Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Arthrobacter phenanthrenivorans type
RT   strain (Sphe3).";
RL   Stand. Genomic Sci. 4:123-130(2011).
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; CP002379; ADX73860.1; -; Genomic_DNA.
DR   RefSeq; WP_013601769.1; NC_015145.1.
DR   ProteinModelPortal; F0M960; -.
DR   STRING; 930171.Asphe3_27410; -.
DR   EnsemblBacteria; ADX73860; ADX73860; Asphe3_27410.
DR   KEGG; apn:Asphe3_27410; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008639; 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:UP000008639};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADX73860.1};
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:UP000008639}.
FT   DOMAIN      261    390       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     52     52       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    282    282       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     329    329       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      52     52       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   405 AA;  42522 MW;  489740720986830E CRC64;
     MTYPATTGEF SAAPANGPRY ERSAVIDLDA IRHNVRRLAA AASPAKVMAV VKADAYGHGA
     VPVARAALEA GASWLGVAHI SEALALRAAG IDAPLLAWLH TPDSNFGAAV AAGVDIGCSG
     WELDRIVAAA REQERPARIH LKVDTGLGRN GATLDTWDHI VGEAMEYQDQ GLLRVVGIFS
     HLAVADEPER PETDQQLATF REVLAVAEDA GVDPEVRHLA NTPATLSRPD THFDLVRVGL
     GIYGLSPFAG QSSAELGLRP AMTLRTLVSQ CKEVPDGQGV SYGLRYHTTG ASTLGLIPMG
     YADGVPRIAT GGPVRVAGRT YPVVGRIAMD QMVIDFGSTV QAGSLLGAEA ELFGDGSDGG
     PTADDWARAA GTINYEIVTR ISPRVPRCFI NEEDKSAASS QEDAA
//
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