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Protein

High-molecular-weight cytochrome c

Gene

hmcA

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi66Iron (heme 1 axial ligand)1
Metal bindingi69Iron (heme 2 axial ligand)1
Binding sitei80Heme 1 (covalent)1
Binding sitei83Heme 1 (covalent)1
Metal bindingi84Iron (heme 1 axial ligand)1
Metal bindingi111Iron (heme 3 axial ligand)1
Binding sitei114Heme 2 (covalent)1
Binding sitei117Heme 2 (covalent)1
Metal bindingi118Iron (heme 2 axial ligand)1
Binding sitei135Heme 3 (covalent)1
Binding sitei138Heme 3 (covalent)1
Metal bindingi139Iron (heme 3 axial ligand)1
Metal bindingi159Iron (heme 4 axial ligand)1
Metal bindingi162Iron (heme 6 axial ligand)1
Binding sitei178Heme 4 (covalent)1
Binding sitei181Heme 4 (covalent)1
Metal bindingi182Iron (heme 4 axial ligand)1
Metal bindingi183Iron (heme 5 axial ligand)1
Binding sitei202Heme 5 (covalent)1
Binding sitei205Heme 5 (covalent)1
Metal bindingi206Iron (heme 5 axial ligand)1
Metal bindingi222Iron (heme 7 axial ligand)1
Binding sitei225Heme 6 (covalent)1
Binding sitei228Heme 6 (covalent)1
Metal bindingi229Iron (heme 6 axial ligand)1
Binding sitei244Heme 7 (covalent)1
Binding sitei247Heme 7 (covalent)1
Metal bindingi248Iron (heme 7 axial ligand)1
Metal bindingi298Iron (heme 8 axial ligand)1
Metal bindingi301Iron (heme 10 axial ligand)1
Binding sitei308Heme 8 (covalent)1
Binding sitei311Heme 8 (covalent)1
Metal bindingi312Iron (heme 8 axial ligand)1
Metal bindingi313Iron (heme 9 axial ligand)1
Binding sitei319Heme 9 (covalent)1
Binding sitei322Heme 9 (covalent)1
Metal bindingi323Iron (heme 9 axial ligand)1
Metal bindingi341Iron (heme 12 axial ligand)1
Binding sitei349Heme 10 (covalent)1
Binding sitei352Heme 10 (covalent)1
Metal bindingi353Iron (heme 10 axial ligand)1
Binding sitei362Heme 11 (covalent)1
Binding sitei365Heme 11 (covalent)1
Metal bindingi366Iron (heme 11 axial ligand)1
Binding sitei378Heme 12 (covalent)1
Binding sitei381Heme 12 (covalent)1
Metal bindingi382Iron (heme 12 axial ligand)1
Metal bindingi449Iron (heme 13 axial ligand)1
Metal bindingi470Iron (heme 11 axial ligand)1
Binding sitei477Heme 13 (covalent)1
Binding sitei480Heme 13 (covalent)1
Metal bindingi481Iron (heme 13 axial ligand)1
Metal bindingi482Iron (heme 14 axial ligand)1
Binding sitei493Heme 14 (covalent)1
Binding sitei496Heme 14 (covalent)1
Metal bindingi497Iron (heme 14 axial ligand)1
Metal bindingi516Iron (heme 16 axial ligand)1
Binding sitei519Heme 15 (covalent)1
Binding sitei522Heme 15 (covalent)1
Metal bindingi523Iron (heme 15 axial ligand)1
Binding sitei536Heme 16 (covalent)1
Binding sitei539Heme 16 (covalent)1
Metal bindingi540Iron (heme 16 axial ligand)1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
High-molecular-weight cytochrome c
Alternative name(s):
Cytochrome CC3
Gene namesi
Name:hmcA
Synonyms:hmc
Ordered Locus Names:DVU_0536
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000000659332 – 545High-molecular-weight cytochrome cAdd BLAST514

Post-translational modificationi

Binds 16 heme groups per subunit. High-spin heme 15 has single axial histidine ligand and the other hemes are low-spin bis-histidinyl coordinated.

Proteomic databases

PaxDbiP24092.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi882.DVU0536.

Structurei

Secondary structure

1545
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 43Combined sources3
Beta strandi45 – 48Combined sources4
Helixi50 – 54Combined sources5
Beta strandi62 – 65Combined sources4
Helixi66 – 75Combined sources10
Helixi80 – 82Combined sources3
Beta strandi93 – 96Combined sources4
Helixi103 – 123Combined sources21
Helixi135 – 138Combined sources4
Beta strandi144 – 147Combined sources4
Helixi156 – 163Combined sources8
Beta strandi172 – 175Combined sources4
Helixi178 – 180Combined sources3
Beta strandi184 – 186Combined sources3
Turni187 – 190Combined sources4
Beta strandi191 – 193Combined sources3
Helixi202 – 204Combined sources3
Helixi217 – 234Combined sources18
Helixi244 – 248Combined sources5
Helixi250 – 253Combined sources4
Beta strandi271 – 275Combined sources5
Beta strandi281 – 285Combined sources5
Beta strandi294 – 297Combined sources4
Helixi298 – 304Combined sources7
Turni309 – 311Combined sources3
Beta strandi312 – 314Combined sources3
Turni320 – 322Combined sources3
Helixi329 – 331Combined sources3
Helixi336 – 341Combined sources6
Beta strandi346 – 348Combined sources3
Helixi349 – 356Combined sources8
Helixi360 – 366Combined sources7
Helixi375 – 378Combined sources4
Turni379 – 381Combined sources3
Beta strandi386 – 388Combined sources3
Helixi390 – 393Combined sources4
Turni394 – 400Combined sources7
Helixi403 – 416Combined sources14
Helixi426 – 428Combined sources3
Beta strandi433 – 435Combined sources3
Beta strandi440 – 442Combined sources3
Beta strandi445 – 447Combined sources3
Helixi449 – 460Combined sources12
Helixi464 – 469Combined sources6
Turni473 – 475Combined sources3
Helixi476 – 479Combined sources4
Helixi493 – 495Combined sources3
Helixi511 – 526Combined sources16
Beta strandi538 – 540Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GWSX-ray2.42A1-545[»]
1H29X-ray2.51A/B/C/D32-545[»]
2CVCX-ray2.00A1-545[»]
ProteinModelPortaliP24092.
SMRiP24092.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24092.

Family & Domainsi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105F1C. Bacteria.
ENOG410XRT9. LUCA.
OMAiTCRVCHH.
OrthoDBiPOG091H0RGX.

Family and domain databases

InterProiIPR002322. Cyt_c_III.
IPR020942. Cyt_c_III_dom.
IPR011346. Cyt_cc3.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamiPF02085. Cytochrom_CIII. 4 hits.
[Graphical view]
PIRSFiPIRSF000026. Cytochrome_cc3. 1 hit.
PRINTSiPR00609. CYTOCHROMEC3.
SUPFAMiSSF48695. SSF48695. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNGRTLLRW AGVLAATAII GVGGFWSQGT TKALPEGPGE KRADLIEIGA
60 70 80 90 100
MERFGKLDLP KVAFRHDQHT TAVTGMGKDC AACHKSKDGK MSLKFMRLDD
110 120 130 140 150
NSAAELKEIY HANCIGCHTD LAKAGKKTGP QDGECRSCHN PKPSAASSWK
160 170 180 190 200
EIGFDKSLHY RHVASKAIKP VGDPQKNCGA CHHVYDEASK KLVWGKNKED
210 220 230 240 250
SCRACHGEKP VDKRPALDTA AHTACISCHM DVAKTKAETG PVNCAGCHAP
260 270 280 290 300
EAQAKFKVVR EVPRLDRGQP DAALILPVPG KDAPREMKGT MKPVAFDHKA
310 320 330 340 350
HEAKANDCRT CHHVRIDTCT ACHTVNGTAD SKFVQLEKAM HQPDSMRSCV
360 370 380 390 400
GCHNTRVQQP TCAGCHGFIK PTKSDAQCGV CHVAAPGFDA KQVEAGALLN
410 420 430 440 450
LKAEQRSQVA ASMLSARPQP KGTFDLNDIP EKVVIGSIAK EYQPSEFPHR
460 470 480 490 500
KIVKTLIAGI GEDKLAATFH IEKGTLCQGC HHNSPASLTP PKCASCHGKP
510 520 530 540
FDADRGDRPG LKAAYHQQCM GCHDRMKIEK PANTACVDCH KERAK
Length:545
Mass (Da):58,901
Last modified:March 1, 1992 - v1
Checksum:i70A620FCC60D070B
GO

Sequence cautioni

The sequence AAS95018 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63807 Genomic DNA. Translation: AAA23355.1.
AE017285 Genomic DNA. Translation: AAS95018.1. Different initiation.
PIRiA39193.
RefSeqiWP_010937842.1. NC_002937.3.
YP_009759.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS95018; AAS95018; DVU_0536.
GeneIDi2795573.
KEGGidvu:DVU0536.
PATRICi32061040. VBIDesVul119526_0512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63807 Genomic DNA. Translation: AAA23355.1.
AE017285 Genomic DNA. Translation: AAS95018.1. Different initiation.
PIRiA39193.
RefSeqiWP_010937842.1. NC_002937.3.
YP_009759.1. NC_002937.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GWSX-ray2.42A1-545[»]
1H29X-ray2.51A/B/C/D32-545[»]
2CVCX-ray2.00A1-545[»]
ProteinModelPortaliP24092.
SMRiP24092.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi882.DVU0536.

Proteomic databases

PaxDbiP24092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS95018; AAS95018; DVU_0536.
GeneIDi2795573.
KEGGidvu:DVU0536.
PATRICi32061040. VBIDesVul119526_0512.

Phylogenomic databases

eggNOGiENOG4105F1C. Bacteria.
ENOG410XRT9. LUCA.
OMAiTCRVCHH.
OrthoDBiPOG091H0RGX.

Miscellaneous databases

EvolutionaryTraceiP24092.

Family and domain databases

InterProiIPR002322. Cyt_c_III.
IPR020942. Cyt_c_III_dom.
IPR011346. Cyt_cc3.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamiPF02085. Cytochrom_CIII. 4 hits.
[Graphical view]
PIRSFiPIRSF000026. Cytochrome_cc3. 1 hit.
PRINTSiPR00609. CYTOCHROMEC3.
SUPFAMiSSF48695. SSF48695. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHMWC_DESVH
AccessioniPrimary (citable) accession number: P24092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 2, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.