ID Q6MB39_PARUW Unreviewed; 370 AA. AC Q6MB39; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 125. DE RecName: Full=Alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183}; DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897, ECO:0000256|PIRNR:PIRNR000183}; GN ORFNames=PC_RS07130 {ECO:0000313|EMBL:CAF24210.1}; OS Protochlamydia amoebophila (strain UWE25). OC Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Parachlamydiales; OC Parachlamydiaceae; Candidatus Protochlamydia. OX NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF24210.1, ECO:0000313|Proteomes:UP000000529}; RN [1] {ECO:0000313|EMBL:CAF24210.1, ECO:0000313|Proteomes:UP000000529} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UWE25 {ECO:0000313|EMBL:CAF24210.1, RC ECO:0000313|Proteomes:UP000000529}; RX PubMed=15073324; DOI=10.1126/science.1096330; RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., RA Mewes H., Wagner M.; RT "Illuminating the evolutionary history of chlamydiae."; RL Science 304:728-730(2004). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine + NAD(+) + H2O = pyruvate + NH4(+) + NADH + H(+); CC Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1; CC Evidence={ECO:0000256|PIRNR:PIRNR000183}; CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}. 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; BX908798; CAF24210.1; -; Genomic_DNA. DR RefSeq; WP_011176033.1; NC_005861.2. DR AlphaFoldDB; Q6MB39; -. DR STRING; 264201.pc1486; -. DR KEGG; pcu:PC_RS07130; -. DR eggNOG; COG0686; Bacteria. DR HOGENOM; CLU_003376_3_0_0; -. DR OrthoDB; 9804592at2; -. DR Proteomes; UP000000529; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0000286; F:L-alanine dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro. DR CDD; cd05305; L-AlaDH; 1. DR FunFam; 3.40.50.720:FF:000049; Alanine dehydrogenase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR InterPro; IPR008141; Ala_DH. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR007886; AlaDH/PNT_N. DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00518; alaDH; 1. DR PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1. DR PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE; 1. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR PIRSF; PIRSF000183; Alanine_dh; 1. DR SMART; SM01002; AlaDh_PNT_C; 1. DR SMART; SM01003; AlaDh_PNT_N; 1. DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000183}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000183-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000183}; KW Reference proteome {ECO:0000313|Proteomes:UP000000529}. FT DOMAIN 4..136 FT /note="Alanine dehydrogenase/pyridine nucleotide FT transhydrogenase N-terminal" FT /evidence="ECO:0000259|SMART:SM01003" FT DOMAIN 148..296 FT /note="Alanine dehydrogenase/pyridine nucleotide FT transhydrogenase NAD(H)-binding" FT /evidence="ECO:0000259|SMART:SM01002" FT ACT_SITE 95 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1" FT ACT_SITE 269 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1" FT BINDING 15 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2" FT BINDING 133 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 197 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 202 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 219 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 238..239 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 266..269 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 278 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" FT BINDING 297..300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3" SQ SEQUENCE 370 AA; 39720 MW; 41E8B7DD0E56169E CRC64; MIIGIPKEIK NHEYRVGATP SMVRLLVDAG HQVFVQSLAG DKIGYNDEMF TRAGAKIVQS AEEVYNSEMI IKVKEPQLSE FPLLKEGQIL FCYLHLAPDP EQTKHLVEKK VVAIAYETVT DVQGRLPLLI PMSEIAGRIA IQVGATSLQL NYGGQGLLLG GVPGVAPAEV VVIGGGVVGT EAARMALGLG ASVTIFDRDL NRLRFLDALY GPTLKTMYSS PLTIEEAVSK AALVIGAVLI PGKTAPKLVT RKMIQKMSPG TVVVDVAIDQ GGCMETSRPT THTEPTYVVD GVLHYCVTNM PGTCARTSTQ ALTNATTEYA LVIANKGWKK ALLDHVGLRH GLNVCFGQIT NESVAYDLGY TYVPAENLLS //