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Database: UniProt/TrEMBL
Entry: A6GYI5_FLAPJ
LinkDB: A6GYI5_FLAPJ
Original site: A6GYI5_FLAPJ 
ID   A6GYI5_FLAPJ            Unreviewed;       817 AA.
AC   A6GYI5;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 105.
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=mur/alr {ECO:0000313|EMBL:CAL43158.1};
GN   OrderedLocusNames=FP1064 {ECO:0000313|EMBL:CAL43158.1};
OS   Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS   JIP02/86).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL43158.1, ECO:0000313|Proteomes:UP000006394};
RN   [1] {ECO:0000313|EMBL:CAL43158.1, ECO:0000313|Proteomes:UP000006394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC   {ECO:0000313|Proteomes:UP000006394};
RX   PubMed=17592475; DOI=10.1038/nbt1313;
RA   Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA   Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA   Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   psychrophilum.";
RL   Nat. Biotechnol. 25:763-769(2007).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; AM398681; CAL43158.1; -; Genomic_DNA.
DR   RefSeq; YP_001295969.1; NC_009613.3.
DR   AlphaFoldDB; A6GYI5; -.
DR   STRING; 402612.FP1064; -.
DR   EnsemblBacteria; CAL43158; CAL43158; FP1064.
DR   KEGG; fps:FP1064; -.
DR   PATRIC; fig|402612.5.peg.1078; -.
DR   eggNOG; COG0770; Bacteria.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_372082_0_0_10; -.
DR   OMA; MVKAFAY; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006394; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 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; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Ligase {ECO:0000313|EMBL:CAL43158.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000006394}.
FT   DOMAIN          691..815
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        486
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        712
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         584
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         761
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         486
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   817 AA;  92307 MW;  93BDC6870E545DEA CRC64;
     MDPLTISLHN IIPILDANFQ GIDENIYYDT ISIDSRSLQN NENTLFFALV GPNNDAHIYI
     GDLISKGVKN FVVTYIPKRL TGKANFLIVK NTLVALQIFA RYYRNLFHFP IIGITGSNGK
     TIVKEWLNFL LSPDYNIIRS PKSYNSQVGV PLSVIAINEN HNLGIFEAGI STKDEMENLQ
     KIIQPTIGIL TNIGTAHDEG FADISEKIKE KLKLFTAVEV LILNKNKTIE TFINKEINTF
     TWSTNDQSAD VFFQKKTLND HALLNITNQG KYFKIKIPFI DEASLENSMH CILVMLYLKY
     DLDTIKHRIS QLFPVEMRLK VKNGINNCTL IDDSYSSDFQ SLKIALDFLE NQKQHLKKTL
     ILSDIYQSGL ENEDLYVRVS QLIISNKINR VICIGGVISK YKNKFLNVIS YLSTNDFIED
     FDNLDFTNET ILIKGSRHFE FEKIVTLLEE KTHETVLEIN LNAISHNLNY FKSKLNPKTK
     IMVMVKAFGY GSGSFEIAKL LAHHKVNYLG VAFADEGIEL RQAGIQLPIM VLNPEMTSFP
     SIIQYNLEPE IYSIRGLKAF IKITQQKELT SYPIHIKINT GMNRLGFDAQ IIPELISILQ
     KHDSVLVKSI LSHLAASDDL AQDIFTRKQI SDFDTISNKI TTKLKINPIR HISNTSAISN
     YPQAQFDMVR LGIGLYGVSN DANETKKLEN VGTLKSIISQ IRNLNSGQSV GYNRRFMVKK
     PTTIATIPIG YADGISRAWG NEVGYVLVNE QKAPIVGSIC MDMLMIDVTK INCSEGNQVI
     IFGKTPSVTT IAKATKTIPY EILTSISSRV KRVFYRE
//
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