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
//