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Database: UniProt/TrEMBL
Entry: A0A067Z4I6_GLUOY
LinkDB: A0A067Z4I6_GLUOY
Original site: A0A067Z4I6_GLUOY 
ID   A0A067Z4I6_GLUOY        Unreviewed;       383 AA.
AC   A0A067Z4I6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 22.
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=alr1 {ECO:0000313|EMBL:AHK71179.1};
GN   ORFNames=GLS_c12820 {ECO:0000313|EMBL:AHK71179.1};
OS   Gluconobacter oxydans DSM 3504.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1288313 {ECO:0000313|EMBL:AHK71179.1, ECO:0000313|Proteomes:UP000031656};
RN   [1] {ECO:0000313|EMBL:AHK71179.1, ECO:0000313|Proteomes:UP000031656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3504 {ECO:0000313|EMBL:AHK71179.1};
RX   PubMed=25267158; DOI=10.1007/s00253-014-6069-9;
RA   Kostner D., Luchterhand B., Junker A., Volland S., Daniel R.,
RA   Buchs J., Liebl W., Ehrenreich A.;
RT   "The consequence of an additional NADH dehydrogenase paralog on the
RT   growth of Gluconobacter oxydans DSM3504.";
RL   Appl. Microbiol. Biotechnol. 99:375-386(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; CP004373; AHK71179.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHK71179; AHK71179; GLS_c12820.
DR   KEGG; goy:GLS_c12820; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000031656; 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:UP000031656};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AHK71179.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      247    373       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     47     47       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      47     47       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   383 AA;  40947 MW;  9B3FC3DD1FAA7F7E CRC64;
     MMSACPDPLW PSYRAGARLT VDLDAIASNY RYLQTLASGA SCAAVVKADA YGLGIERVAP
     VLENAGATDF FVAHVDEGIR LRSVVSDKAR ITVLHGPRPG ASGDCVRYGL RPVLNSLEQI
     ALWRDEGSWT GGLPEAALQV DSGMLRFGLS DADLETLQAD KGLVDGLHVG LVMSHLACAD
     TPDHPANQAQ KDRLLQMSAR LPPAPLSLSA SSGIFLGTDY HLDVVRPGAA LYGIAPNRTG
     PNPLSPVVRL QAHVLQIREI LPGEGVGYGL TYRPDRVRRI ATVAVGYADG FSRHGAGQGC
     AWFEDIRLPI LGRVSMDSLI VDISEVPEGK LGPDMMVDLI GPRRSVDDVA EAAGTIGYEV
     LTSLGHRFHR EYVGNQENPS RGD
//
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