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Database: UniProt/TrEMBL
Entry: A0A0D5LVB1_9RHIZ
LinkDB: A0A0D5LVB1_9RHIZ
Original site: A0A0D5LVB1_9RHIZ 
ID   A0A0D5LVB1_9RHIZ        Unreviewed;       389 AA.
AC   A0A0D5LVB1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 19.
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=TM49_14580 {ECO:0000313|EMBL:AJY48234.1};
OS   Martelella endophytica.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Aurantimonadaceae; Martelella.
OX   NCBI_TaxID=1486262 {ECO:0000313|EMBL:AJY48234.1, ECO:0000313|Proteomes:UP000032611};
RN   [1] {ECO:0000313|EMBL:AJY48234.1, ECO:0000313|Proteomes:UP000032611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6887 {ECO:0000313|EMBL:AJY48234.1};
RX   PubMed=25953177;
RA   Khan A., Khan H., Chung E.J., Hossain M.T., Chung Y.R.;
RT   "Complete Genome Sequence of Martelella endophytica YC6887, Which Has
RT   Antifungal Activity Associated with a Halophyte.";
RL   Genome Announc. 3:0-0(2015).
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; CP010803; AJY48234.1; -; Genomic_DNA.
DR   RefSeq; WP_045685276.1; NZ_CP010803.1.
DR   EnsemblBacteria; AJY48234; AJY48234; TM49_14580.
DR   KEGG; mey:TM49_14580; -.
DR   PATRIC; fig|1486262.3.peg.3013; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000032611; 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:UP000032611};
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:UP000032611}.
FT   DOMAIN      249    386       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     53     53       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    270    270       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     148    148       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      53     53       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   389 AA;  41299 MW;  5C0FD58C4FF949D4 CRC64;
     MNDYSNDLID DEDESQVFDT APARLTVDLG AIVENWKTMR ALSGGARTAA VLKADAYGLG
     IEDVGEALYA AGAQDFFVAV PEEGATLREF APDARIFVLS GMWPGTEALF FSYDLVPVLA
     SEEQIAFFTS VVPGPYPCAL QVDTGFNRLG LTPEEAIAFA GDASRPANIE PVLVLSHLAC
     GDDPASPMNV EQLARFSQVA NAFEGIEASL SASAGIFLGS DYHFDLTRPG IALYGGDSQV
     GTSKRLRPVA TAEARIVQIR SARAGETVSY GATTTLSRDS RLAIVAAGYA DGYHRALSGS
     GTPLRGAVEQ GGYGFVAGHR VPIAGRITMD MTIFDVTDVP ERTIRAGDYI ELIGPNMPLD
     EAAAAAGTIG YEMLTSLGLR YTRRYTQPD
//
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