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Database: UniProt/TrEMBL
Entry: A0A077FHB9_9RICK
LinkDB: A0A077FHB9_9RICK
Original site: A0A077FHB9_9RICK 
ID   A0A077FHB9_9RICK        Unreviewed;       371 AA.
AC   A0A077FHB9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 21.
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=dadX {ECO:0000313|EMBL:AIL64787.1};
GN   ORFNames=NOVO_01960 {ECO:0000313|EMBL:AIL64787.1};
OS   Rickettsiales bacterium Ac37b.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales.
OX   NCBI_TaxID=1528098 {ECO:0000313|EMBL:AIL64787.1, ECO:0000313|Proteomes:UP000028936};
RN   [1] {ECO:0000313|EMBL:AIL64787.1, ECO:0000313|Proteomes:UP000028936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac37b {ECO:0000313|EMBL:AIL64787.1,
RC   ECO:0000313|Proteomes:UP000028936};
RA   Felsheim R.F., Kurtti T.J., Johnson S., Labruna M.B., Munderloh U.G.;
RT   "Genome sequence of a novel Rickettsiales species cultured from
RT   Amblyomma cajennense.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP009217; AIL64787.1; -; Genomic_DNA.
DR   RefSeq; WP_038602112.1; NZ_CP009217.1.
DR   EnsemblBacteria; AIL64787; AIL64787; NOVO_01960.
DR   KEGG; rbt:NOVO_01960; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000028936; 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:UP000028936};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AIL64787.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028936}.
FT   DOMAIN      237    363       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    258    258       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     306    306       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   371 AA;  41546 MW;  24BD437EBE21A607 CRC64;
     MTSYADAILN VDLNSIVYNY LFLKKKLNTV ECGAVVKANA YGIGANHVAS TLAKYGCKHF
     FVANLEEAIS LRAILTKQYN IYVLHGVFPN QEQEFIHYNL TPILNDIYQI KIWNCFASTK
     KIQLPAILYI DTGLSRLGLT TYDALDLFYN QTLVANLNIL YLMSHLSAAD NPTHPLNAEQ
     LKKMSIIQKY MPNTHITFVN SSGIFLGTNY HFHLARPGMA LYGLNPTPQS KNPMHNVIYL
     SSKIIQVRNN IKQSPVGYGG SYYAERNSVI ATVAIGYADG YFRSLSNNSI CYINGYKAPV
     IGRVSMDLIT LDVTNVPAHF IYPGQSVEII GDNITVDQLA KYANTLGYEI LTNLGHRFKL
     VYNIDIQLND I
//
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