ID A0A1L8CLS4_9PROT Unreviewed; 368 AA.
AC A0A1L8CLS4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=MMIC_P0811 {ECO:0000313|EMBL:GAV19853.1};
OS Mariprofundus micogutta.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=1921010 {ECO:0000313|EMBL:GAV19853.1, ECO:0000313|Proteomes:UP000231632};
RN [1] {ECO:0000313|EMBL:GAV19853.1, ECO:0000313|Proteomes:UP000231632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ET2 {ECO:0000313|EMBL:GAV19853.1,
RC ECO:0000313|Proteomes:UP000231632};
RX PubMed=27766355; DOI=10.1007/s00203-016-1307-4;
RA Makita H., Tanaka E., Mitsunobu S., Miyazaki M., Nunoura T., Uematsu K.,
RA Takaki Y., Nishi S., Shimamura S., Takai K.;
RT "Mariprofundus micogutta sp. nov., a novel iron-oxidizing
RT zetaproteobacterium isolated from a deep-sea hydrothermal field at the
RT Bayonnaise knoll of the Izu-Ogasawara arc, and a description of
RT Mariprofundales ord. nov. and Zetaproteobacteria classis nov.";
RL Arch. Microbiol. 199:335-346(2017).
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 -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000183}.
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:GAV19853.1}.
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DR EMBL; BDFD01000005; GAV19853.1; -; Genomic_DNA.
DR RefSeq; WP_072659257.1; NZ_BDFD01000005.1.
DR AlphaFoldDB; A0A1L8CLS4; -.
DR STRING; 1921010.MMIC_P0811; -.
DR OrthoDB; 5288847at2; -.
DR Proteomes; UP000231632; Unassembled WGS sequence.
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:InterPro.
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; 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; 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}.
FT DOMAIN 4..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..300
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 273
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 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 270..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
FT BINDING 282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000183-3"
SQ SEQUENCE 368 AA; 39336 MW; 2E6E925470DE2D5A CRC64;
MRIGIPKEIK NHEHRVALSP AGAAVLIAAG HQVVVQSEAG LDSGYSDDSY LRAGAEIVTD
AWQAWGQELV VKVKEPQQIE YEYLRGDLIL FTFLHLAAFP ELAGVLRDKK TCAIAYETVQ
TDAGLLPLLK PMSEVAGRVA VQLGASFLQK ENGTAFPGKG CLPCAIGTAP AMHAVILGAG
NVGMNAADAA AGLGARVTLL ERDEKRIKQL QRETHKNITV MHFSHDCFYS LLPDCDLLIG
ATLIPGKHAP ELLGRSDLRQ MQNGSVFIDV SIDQGGISET CRATSYDEPV YVEEGVIHCC
LPNLPAAVPQ TSTRALTEIT LPYIQSVADL GVDGVIKSHP ALQRGINTLA GEIIHPAVAA
SLSNKVIR
//
