ID K5BBI8_MYCHD Unreviewed; 371 AA.
AC K5BBI8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 Name=ald {ECO:0000313|EMBL:EKF24065.1};
GN Synonyms=ald_2 {ECO:0000313|EMBL:VCT90695.1};
GN ORFNames=C731_1825 {ECO:0000313|EMBL:EKF24065.1}, MHAS_02404
GN {ECO:0000313|EMBL:VCT90695.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF24065.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF24065.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 {ECO:0000313|EMBL:EKF24065.1}, and DSM 44199 / CIP
RC 105218 / JCM 12690 / 3849 {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
RN [2] {ECO:0000313|EMBL:VCT90695.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mhassiacum {ECO:0000313|EMBL:VCT90695.1};
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000268660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000268660};
RX PubMed=30701245; DOI=10.1128/mra.01522-18;
RA Sanchez M., Blesa A., Sacristan-Horcajada E., Berenguer J.;
RT "Complete genome sequence of Mycolicibacterium hassiacum DSM 44199.";
RL Microbiol. Resour. Announc. 8:e01522-e01522(2019).
CC -!- FUNCTION: Catalyzes the reversible reductive amination of pyruvate to
CC L-alanine. {ECO:0000256|PIRNR:PIRNR000183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate;
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 -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005206, ECO:0000256|PIRNR:PIRNR000183}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}.
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DR EMBL; AMRA01000046; EKF24065.1; -; Genomic_DNA.
DR EMBL; LR026975; VCT90695.1; -; Genomic_DNA.
DR RefSeq; WP_005626753.1; NZ_LR026975.1.
DR AlphaFoldDB; K5BBI8; -.
DR STRING; 1122247.GCA_000379865_04821; -.
DR KEGG; mhas:MHAS_02404; -.
DR PATRIC; fig|1122247.3.peg.1756; -.
DR eggNOG; COG0686; Bacteria.
DR OrthoDB; 9804592at2; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR Proteomes; UP000268660; Chromosome 1.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05305; L-AlaDH; 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; IPR008142; AlaDH/PNT_CS1.
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; 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; PS00836; ALADH_PNT_1; 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:UP000006265}.
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..297
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT ACT_SITE 96
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-1"
FT ACT_SITE 270
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 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-2"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 178..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 239..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 267..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 298..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-4"
SQ SEQUENCE 371 AA; 38302 MW; 6485D672B3EAF825 CRC64;
MRVGIPTEIK NNEYRVAITP AGVAELVHRG HEVIIQSGAG EGSAIPDADF VKAGAGLVAG
ADQVWAEADL VLKVKEPIAA EYHRMRAGQT LFTYLHLAAS KECTEALLAA GTTAIAYETV
QTADGALPLL APMSEVAGRL AAQVGAYHLM RSHGGRGVLM GGVPGVAPAD VVVIGGGTAG
YNAARVAAGM GAQVTVFDVN IDRLRAIDAE SRGRLQTRFS TRTELEDAVT RADLVIGAVL
VPGAKAPKLV SNSTVAQMQP GAVLVDIAID QGGCFEDSHP TTHDDPTFGV HDTLFYCVAN
MPGAVPRTST FALTNATLPY VLALADHGWR AACQADPALA AGLSTHEGAL LSATVAADLD
LPFTDPAEVL A
//
