ID M7NKB2_9MICC Unreviewed; 471 AA.
AC M7NKB2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=ADIAG_01742 {ECO:0000313|EMBL:EMQ98983.1};
OS Paeniglutamicibacter gangotriensis Lz1y.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paeniglutamicibacter.
OX NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ98983.1, ECO:0000313|Proteomes:UP000012015};
RN [1] {ECO:0000313|EMBL:EMQ98983.1, ECO:0000313|Proteomes:UP000012015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lz1y {ECO:0000313|EMBL:EMQ98983.1,
RC ECO:0000313|Proteomes:UP000012015};
RX PubMed=23766407;
RA Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT Station Dakshin Gangotri.";
RL Genome Announc. 1:e00347-e00313(2013).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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:EMQ98983.1}.
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DR EMBL; AOCK01000004; EMQ98983.1; -; Genomic_DNA.
DR RefSeq; WP_007270932.1; NZ_AOCK01000004.1.
DR AlphaFoldDB; M7NKB2; -.
DR STRING; 1276920.ADIAG_01742; -.
DR PATRIC; fig|1276920.7.peg.1744; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000012015; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:EMQ98983.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000012015};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EMQ98983.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 165..202
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 82..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 49030 MW; 0F743973BABFEF12 CRC64;
MSMKTFLLPD LGEGLTEAEL VKWLVAVGDT VVIDQPIAEV ETAKSMVEVP SPYAGTVHEL
HGTVGEMVLV DTPLFSVLEE GSAAPAAEPQ PAAPEREVAQ SYREEERAGT QEPASEGSGN
VLIGYGTPEG LSAKARKRRP RQSAGTPLAP AARGEAVAPR RAPLVISPLV RKLARELGIN
IAEVTGSGAG GLVLRSDIEA AAAVRSAPAA PASAPVAPAT TPAPAQPAGD IDSRSGLPIA
SRTPITGVRK TIASAMTRSR SEIPEATVWV DVDVSNLLAL RSDMKAKDPK NTPGLLAFIA
RFVVAGLQKY PELNSRIEQS AEGPAEIVGF EGINLGIAAQ TDRGLMVPSI RNAQNLSARG
LNAELARLTE VTRAGKASVA ELTSGTFTLN NYGVFGVDGS AAIINYPEVA ILGVGRIIDK
PWVVEGELAV RKLTELTLAF DHRACDGGTA AGFLRFVADA MENPAAVLAD L
//
