ID M8D5X0_9BACI Unreviewed; 472 AA.
AC M8D5X0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Lactate utilization protein B {ECO:0000256|HAMAP-Rule:MF_02103};
GN Name=lutB {ECO:0000256|HAMAP-Rule:MF_02103};
GN ORFNames=H919_06511 {ECO:0000313|EMBL:EMT46227.1};
OS Anoxybacillus flavithermus AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1297581 {ECO:0000313|EMBL:EMT46227.1, ECO:0000313|Proteomes:UP000012085};
RN [1] {ECO:0000313|EMBL:EMT46227.1, ECO:0000313|Proteomes:UP000012085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT46227.1,
RC ECO:0000313|Proteomes:UP000012085};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Anoxybacillus flavithermus AK1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EMT46227.1, ECO:0000313|Proteomes:UP000012085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT46227.1,
RC ECO:0000313|Proteomes:UP000012085};
RX PubMed=26044438;
RA Khalil A., Sivakumar N., Qarawi S.;
RT "Genome Sequence of Anoxybacillus flavithermus Strain AK1, a Thermophile
RT Isolated from a Hot Spring in Saudi Arabia.";
RL Genome Announc. 3:e00604-15(2015).
CC -!- FUNCTION: Is involved in L-lactate degradation and allows cells to grow
CC with lactate as the sole carbon source. Has probably a role as an
CC electron transporter during oxidation of L-lactate. {ECO:0000256|HAMAP-
CC Rule:MF_02103}.
CC -!- SIMILARITY: Belongs to the LutB/YkgF family. {ECO:0000256|HAMAP-
CC Rule:MF_02103}.
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:EMT46227.1}.
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DR EMBL; APCD01000006; EMT46227.1; -; Genomic_DNA.
DR RefSeq; WP_003396816.1; NZ_APCD01000006.1.
DR AlphaFoldDB; M8D5X0; -.
DR PATRIC; fig|1297581.3.peg.1340; -.
DR Proteomes; UP000012085; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019516; P:lactate oxidation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR HAMAP; MF_02103; LutB; 1.
DR InterPro; IPR004452; 4Fe-4S-bd.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR024185; FTHF_cligase-like_sf.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR003741; LUD_dom.
DR InterPro; IPR022825; LutB.
DR InterPro; IPR024569; LutB_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR00273; LutB/LldF family L-lactate oxidation iron-sulfur protein; 1.
DR PANTHER; PTHR47153; LACTATE UTILIZATION PROTEIN B; 1.
DR PANTHER; PTHR47153:SF2; LACTATE UTILIZATION PROTEIN B; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR Pfam; PF02589; LUD_dom; 1.
DR Pfam; PF11870; LutB_C; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02103};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_02103};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02103};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_02103};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02103};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_02103};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_02103}.
FT DOMAIN 303..334
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02103"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02103"
FT BINDING 319
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02103"
FT BINDING 323
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02103"
FT BINDING 366
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02103"
FT BINDING 369
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02103"
FT BINDING 373
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02103"
SQ SEQUENCE 472 AA; 52582 MW; 28A87B48F2C7A708 CRC64;
MALKINMGEF HERVEKGIHN TFMRGAVAGA QERLRTRRLE AAAELGNWEE WRALGEEIRQ
HTLENLDYYL MQLSENVKKR GGHVFFAQTA EEANDYICRV VASKQAKKIV KSKSMVTEEI
HMNAALEKLG CEVIETDLGE YILQVDDHDP PSHIVAPALH KNKEQIRDVF KEKLAYTKTE
KPEELALHAR HMLRHEYMTA DVGITGCNFA IAESGSITLV TNEGNADLVT ALPKTQITVM
GMERIVPTFE EMEVLVSLLT RSAVGQKLTS YITVLTGPRD QEEVDGPEEF HLVIVDNGRS
DILGTEFQPV LQCIRCAACV NVCPVYRHIG GHSYGSIYSG PIGAVLSPLL GGYDDYKELP
YASTLCAACT EACPVKIPLH ELLLKHRQTI VEREGKAPIS EKLAMKAFGL GAASSLLYKI
GSKVAPSAMN PFTVNDRISK GPGPLKAWTD IREFPAPEKE RFRDWLKQRG NE
//
