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Database: UniProt/TrEMBL
Entry: B2RK18_PORG3
LinkDB: B2RK18_PORG3
Original site: B2RK18_PORG3 
ID   B2RK18_PORG3            Unreviewed;       823 AA.
AC   B2RK18;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 95.
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=PGN_1194 {ECO:0000313|EMBL:BAG33713.1};
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947 {ECO:0000313|EMBL:BAG33713.1, ECO:0000313|Proteomes:UP000008842};
RN   [1] {ECO:0000313|EMBL:BAG33713.1, ECO:0000313|Proteomes:UP000008842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
RC   2561 {ECO:0000313|Proteomes:UP000008842};
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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; AP009380; BAG33713.1; -; Genomic_DNA.
DR   RefSeq; WP_012458093.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RK18; -.
DR   GeneID; 29256399; -.
DR   KEGG; pgn:PGN_1194; -.
DR   eggNOG; COG0770; Bacteria.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_372082_0_0_10; -.
DR   OMA; MVKAFAY; -.
DR   OrthoDB; 9801978at2; -.
DR   BioCyc; PGIN431947:G1G2V-1366-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008842; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}.
FT   DOMAIN          697..821
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        494
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        718
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         592
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         767
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         494
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   823 AA;  91841 MW;  F114D52642190518 CRC64;
     MFLFSELCRR LSPDAVRIVS DHRIVHLLTD SRTLSEPATT LFFALRTTSG DGHLYIRDLY
     DKGVRSFVIS DPSKDLMEKM PQANWMRVAH PLDALQRIAA LRRSMFDIPV IGITGSNGKT
     IVKEFLYQLL RKDYRIVRSP RSYNSQIGVP LSVWQMAEEH TLGIFEAGIS QMGEMERLES
     IICPSYGIIT NIGGAHQENF PDIKTKLEEK LRLFPHCHTI VYNGDCEEIA AAISFCGLAR
     AGVSWSRTKP EAHLYVCRLE SKDNRTEIDF RCLGKDYSLV LPFTDAASIE DIIHCITLIS
     VLCPEVLSAR KRFASLEPVE MRMEVKAGDH GNTIINDVYS NDVYSLTLAL DFQRRRTAET
     CLKKVLILSD ILQSGMPPEE LYRHVAGQLQ VYALDFFVGI GEEIASHRTC FAGMSAVFFK
     DVAAFLTSGE IERFSNSCIL LKGARKYRFE QITERLVQQV HETALRINLS AIIHNLNFYR
     NLVPSGTKTI CMVKAQGYGV GSYELVKTLQ EHRVDYIAVA VADEGKELRE RGISMPIVVM
     NPQRNAFQTL IDYGLEPEIY SFALLASFSE TVVRNGLVGY PVHIKIDTGM HRLGFLPSDM
     TRLGEILAKD AGLSIRSVFT HLAGADDPDL DDFTRSQLLS FDAAFASLSS LLGYIPLRHV
     LNTAGVERFA DYHADMIRLG IGLYGVTASG VQGLRPVATL MTTILQIKDI SSSDTVGYGR
     KGRVQQPSRI AIIPIGYADG LDRRLSCGVG EVLVRGHRCP IVGNVCMDIC MIDVTGMPAE
     EGDPVVVFGE ELPIEEVAHK MNTIPYEVLT GISPRVRRVY FQE
//
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