ID A0A0C3NFF9_9PORP Unreviewed; 815 AA.
AC A0A0C3NFF9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=BA92_07395 {ECO:0000313|EMBL:KIO44837.1};
OS Sanguibacteroides justesenii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Sanguibacteroides.
OX NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO44837.1, ECO:0000313|Proteomes:UP000031980};
RN [1] {ECO:0000313|EMBL:KIO44837.1, ECO:0000313|Proteomes:UP000031980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO44837.1,
RC ECO:0000313|Proteomes:UP000031980};
RA Sydenham T.V., Hasman H., Justensen U.S.;
RT "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT genome.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIO44837.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPIU01000038; KIO44837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3NFF9; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000031980; Unassembled WGS sequence.
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; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR Pfam; PF01225; Mur_ligase; 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}; Reference proteome {ECO:0000313|Proteomes:UP000031980}.
FT DOMAIN 689..813
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 487
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 710
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 585
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 759
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 487
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 815 AA; 92595 MW; 1CA1F5BF68E51F00 CRC64;
MMYSIEEIAR VIRGDLKKGC PVTISEYGID SRSVIYADQT LFFALKGQNH DAHDYILSLY
ENGVRAFVIH EYRSEFDRLT EANFIRVDDV LSALQQLAAH YRQQSKAEII GITGSNGKTI
VKEWLSQLLM ENYRVYRSPR SYNSQVGVPL SLLGIEEETE IAVIEAGISQ KGEMQRLEQM
IRPDIGLFTH IGEAHDENFT STEEKLTEKA KLFTSCKTLV GQAGEVLKFI KKQLPDRVRL
FLWGDSPEAI VKTETLDIDA KSRQVRITHG NISFLLTIPF PDAASFENTM NAVCVLLLKG
IQPSSITRLV KHLSSIAMRM EIKEGINNCI LINDYYNSDP ASFQLALNSL SIQDPHKERV
VILSDFMDIS EDKQTLYKSI AMLLQQAKIS CFIGIGKELR EYQHYFTVDN SRFYENTEQF
LKQENRNNFK NQVILIKGAR RFQFEFIAGF LQKQSHGTIL EVDLDAMVHN LNYFRSLTSA
KLAVMVKAFS YGSGSKEIAS LLQYHRVDYL MVAFADEGIE LRAAGITLPI AVMNPEREAF
DNMITFGLEP EIYALDILED FEKALGKHGI KHFPVHVKLN TGMNRSGFDE KDLPELLRFF
NRPRTVYIRS LFSHLAGSDE SIHDEFTLNQ IHLFENMTTT IQAHFNYKIW RHILNSAGIE
RFPQYHFDMV RLGIGLHGIS SDHALLRPVS TFKTHISSIR EVPTGQSIGY GRKSYTDRPS
RIAVIPVGYA DGLNRHLSNR VGEVYVKGKK APIIGNICMD TCMIDITDTD ALVGEEVEIF
GKHIPVTEIA DKLGTIPYEI LTGVSSRVKR VYYKE
//
