ID D8ACH0_ECOMS Unreviewed; 268 AA.
AC D8ACH0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Protein FixA {ECO:0000256|HAMAP-Rule:MF_01055};
GN Name=fixA {ECO:0000256|HAMAP-Rule:MF_01055};
GN ORFNames=HMPREF9530_04262 {ECO:0000313|EMBL:EFK19169.1};
OS Escherichia coli (strain MS 21-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK19169.1, ECO:0000313|Proteomes:UP000005688};
RN [1] {ECO:0000313|EMBL:EFK19169.1, ECO:0000313|Proteomes:UP000005688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK19169.1,
RC ECO:0000313|Proteomes:UP000005688};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for anaerobic carnitine reduction. May bring
CC reductant to CaiA. {ECO:0000256|HAMAP-Rule:MF_01055}.
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_01055}.
CC -!- SUBUNIT: Heterodimer of FixA and FixB. {ECO:0000256|HAMAP-
CC Rule:MF_01055}.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family.
CC {ECO:0000256|ARBA:ARBA00007557, ECO:0000256|HAMAP-Rule:MF_01055}.
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:EFK19169.1}.
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DR EMBL; ADTR01000389; EFK19169.1; -; Genomic_DNA.
DR AlphaFoldDB; D8ACH0; -.
DR HOGENOM; CLU_060196_2_2_6; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000005688; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01055; FixA; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR023463; FixA.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT; 1.
DR PANTHER; PTHR21294:SF22; PROTEIN FIXA; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01055};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01055}.
FT DOMAIN 34..227
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
SQ SEQUENCE 268 AA; 28398 MW; 9B51F42DE3495556 CRC64;
MNDVSFMISG DAMKIITCYK CVPDEQDIAV NNADGSLDFS KADAKISQYD LNAIEAACQL
KQQAAEGQVT ALSVGGKALT NAKGRKDVLS RGPDELIVVI DDQFEQALPQ QTASALAAAA
QKAGFDLILC GDGSSDLYAQ QVGLLVGEIL NIPAVNGVSK IISLTADTLT VERELEDETE
TLSIPLPAVV AVSTDINSPQ IPSMKAILGA AKKPVQVWSA ADIGFNAEAA WSEQQVAAPK
QRERQRIVIE GDGEEQIAAF AENLRKVI
//
