ID A0A3S0A583_9RICK Unreviewed; 358 AA.
AC A0A3S0A583;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=alanine racemase {ECO:0000256|ARBA:ARBA00013089};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN Name=alr {ECO:0000313|EMBL:RST63776.1};
GN ORFNames=EIC27_05190 {ECO:0000313|EMBL:RST63776.1};
OS Candidatus Aquarickettsia rohweri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Aquarickettsia.
OX NCBI_TaxID=2602574 {ECO:0000313|EMBL:RST63776.1, ECO:0000313|Proteomes:UP000279470};
RN [1] {ECO:0000313|Proteomes:UP000279470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a_cerv_44 {ECO:0000313|Proteomes:UP000279470};
RA Klinges J.G., Rosales S.M., Mcminds R., Shaver E.C., Shantz A.,
RA Peters E.C., Burkepile D.E., Silliman B.R., Vega Thurber R.L.;
RT "Phylogenetic, genomic, and biogeographic characterization of a novel and
RT ubiquitous marine invertebrate-associated Rickettsiales parasite,
RT Candidatus Marinoinvertebrata rohwerii, gen. nov., sp. nov.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000316};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|ARBA:ARBA00007880}.
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:RST63776.1}.
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DR EMBL; RXFM01000074; RST63776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0A583; -.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000279470; Unassembled WGS sequence.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine 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 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 PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RST63776.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000279470}.
FT DOMAIN 231..357
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 38
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 358 AA; 41145 MW; 6AC21ABCC6B42A93 CRC64;
MFDKYQYIQV NLEHLKKNYL KLKSFLNSNK TICSAVVKAN AYGLGIKEVS QALYEVGCRN
FWVTNLKEAF LVRCVSIESN IYIFQGINSY EELEVIKENN FIPVVSSIEQ LNLINLYVKD
KVNIVLNFDT GIGREGVQIE EIKQLNLEKC KIELIMSHLS CSEQKEHFLN KEQLDLFKNI
QDLFVDAKFT LANSGGIFLG HEYHFNMVRP GSALYGVNIL EDNNDVKMLN VVEFYASVLN
RKIFYKKQYI GYNATYKVNK GDKVLIINAG YYDGYRRILS NKSMVYSKGY FLPVIGIVSM
NMIAVNANAL PESLFKKIKS VELIGEKITI KEIAKWANTD QREILTNISS SSRRIYIK
//
